An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.
An enzyme that oxidizes galactose in the presence of molecular oxygen to D-galacto-hexodialdose. It is a copper protein. EC 1.1.3.9.
D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.
Phosphoric acid esters of galactose.
A group of inherited enzyme deficiencies which feature elevations of GALACTOSE in the blood. This condition may be associated with deficiencies of GALACTOKINASE; UDPGLUCOSE-HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; or UDPGLUCOSE 4-EPIMERASE. The classic form is caused by UDPglucose-Hexose-1-Phosphate Uridylyltransferase deficiency, and presents in infancy with FAILURE TO THRIVE; VOMITING; and INTRACRANIAL HYPERTENSION. Affected individuals also may develop MENTAL RETARDATION; JAUNDICE; hepatosplenomegaly; ovarian failure (PRIMARY OVARIAN INSUFFICIENCY); and cataracts. (From Menkes, Textbook of Child Neurology, 5th ed, pp61-3)
A nucleoside diphosphate sugar which can be epimerized into UDPglucose for entry into the mainstream of carbohydrate metabolism. Serves as a source of galactose in the synthesis of lipopolysaccharides, cerebrosides, and lactose.
A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.
An enzyme that catalyzes reversibly the formation of galactose 1-phosphate and ADP from ATP and D-galactose. Galactosamine can also act as the acceptor. A deficiency of this enzyme results in GALACTOSEMIA. EC 2.7.1.6.
An enzyme that catalyzes the synthesis of UDPgalactose from UTP and galactose-1-phosphate. It is present in low levels in fetal and infant liver, but increases with age, thereby enabling galactosemic infants who survive to develop the capacity to metabolize galactose. EC 2.7.7.10.
A naturally occurring product of plants obtained following reduction of GALACTOSE. It appears as a white crystalline powder with a slight sweet taste. It may form in excess in the lens of the eye in GALACTOSEMIAS, a deficiency of GALACTOKINASE.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
Fucose is a deoxyhexose sugar, specifically a L-configuration 6-deoxygalactose, often found as a component of complex carbohydrates called glycans in various glycoproteins and glycolipids within the human body.
A disaccharide of GLUCOSE and GALACTOSE in human and cow milk. It is used in pharmacy for tablets, in medicine as a nutrient, and in industry.
Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)
Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
Hexoses are simple monosaccharides, specifically six-carbon sugars, which include glucose, fructose, and galactose, and play crucial roles in biological processes such as energy production and storage, and structural components of cells.
The N-acetyl derivative of galactosamine.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
An enzyme that catalyzes the transfer of UMP from UDPglucose to galactose 1-phosphate, forming UDPgalactose and glucose 1-phosphate. Deficiency in this enzyme is the major cause of GALACTOSEMIA. EC 2.7.7.12.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
The characteristic 3-dimensional shape of a carbohydrate.
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
Methylgalactosides are disaccharides consisting of a galactose molecule linked to a methyl group through a glycosidic bond, found in certain food sources and potentially used as sweeteners.
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
An enzyme that catalyzes the conversion of alpha D-glucose 1-phosphate to alpha D-glucose 6-phosphate. EC 5.4.2.2.
Glucosamine is a naturally occurring amino sugar that plays a crucial role in the formation and maintenance of various tissues, particularly in the synthesis of proteoglycans and glycosaminoglycans, which are essential components of cartilage and synovial fluid in joints.
An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.
SUGARS containing an amino group. GLYCOSYLATION of other compounds with these amino sugars results in AMINOGLYCOSIDES.
A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.
Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)
Uridine Diphosphate (UDP) sugars are nucleotide sugars that serve as essential glycosyl donors in the biosynthesis of various glycoconjugates, including proteoglycans and glycoproteins.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Glycosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of galactose with an alcohol to form an acetal. They include both alpha- and beta-galactosides.
A class of inorganic or organic compounds that contain the borohydride (BH4-) anion.
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.
The N-acetyl derivative of glucosamine.
Endogenous glycoproteins from which SIALIC ACID has been removed by the action of sialidases. They bind tightly to the ASIALOGLYCOPROTEIN RECEPTOR which is located on hepatocyte plasma membranes. After internalization by adsorptive ENDOCYTOSIS they are delivered to LYSOSOMES for degradation. Therefore receptor-mediated clearance of asialoglycoproteins is an important aspect of the turnover of plasma glycoproteins. They are elevated in serum of patients with HEPATIC CIRRHOSIS or HEPATITIS.
Hexosamines are amino sugars that are formed by the substitution of an amino group for a hydroxyl group in a hexose sugar, playing crucial roles in various biological processes such as glycoprotein synthesis and protein folding.
Arabinose is a simple, pentose sugar (a monosaccharide with five carbon atoms) that is a constituent of various polysaccharides and glycosides, particularly found in plant tissues and some microorganisms, and can be metabolized in humans as a source of energy through the pentose phosphate pathway.
Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)
A methylpentose whose L- isomer is found naturally in many plant glycosides and some gram-negative bacterial lipopolysaccharides.
Neuraminic acids are a family of nine-carbon sugars (sialic acids) that are commonly found as terminal residues on glycoproteins and gangliosides in animal tissues, playing crucial roles in various biological processes including cell recognition, inflammation, and bacterial/viral infectivity.
A family of calcium-binding alpha-globulins that are synthesized in the LIVER and play an essential role in maintaining the solubility of CALCIUM in the BLOOD. In addition the fetuins contain aminoterminal cystatin domains and are classified as type 3 cystatins.
Lipids containing at least one monosaccharide residue and either a sphingoid or a ceramide (CERAMIDES). They are subdivided into NEUTRAL GLYCOSPHINGOLIPIDS comprising monoglycosyl- and oligoglycosylsphingoids and monoglycosyl- and oligoglycosylceramides; and ACIDIC GLYCOSPHINGOLIPIDS which comprises sialosylglycosylsphingolipids (GANGLIOSIDES); SULFOGLYCOSPHINGOLIPIDS (formerly known as sulfatides), glycuronoglycosphingolipids, and phospho- and phosphonoglycosphingolipids. (From IUPAC's webpage)
Galactosamine is a type of amino monosaccharide that is a key component of many glycosaminoglycans, and is commonly found in animal tissues, often used in research and pharmaceutical applications for its role in cellular metabolism and synthesis of various biological molecules.
A strong oxidizing agent.
Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Polysaccharides found in bacteria and in capsules thereof.
A disaccharide consisting of one galactose and one glucose moiety in an alpha (1-6) glycosidic linkage.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)
Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.
An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-galactosides including galactose oligosaccharides, galactomannans, and galactolipids.
The rate dynamics in chemical or physical systems.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Xylose is a monosaccharide, a type of sugar, that is commonly found in woody plants and fruits, and it is used in medical testing to assess the absorptive capacity of the small intestine.
An order of gram-positive, primarily aerobic BACTERIA that tend to form branching filaments.
A monosaccharide in sweet fruits and honey that is soluble in water, alcohol, or ether. It is used as a preservative and an intravenous infusion in parenteral feeding.
An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)
A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
Hexosephosphates are sugar phosphate molecules, specifically those derived from hexoses (six-carbon sugars), such as glucose-6-phosphate and fructose-6-phosphate, which play crucial roles in various metabolic pathways including glycolysis, gluconeogenesis, and the pentose phosphate pathway.
The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
An enzyme that catalyzes the formation of UDPglucose from UTP plus glucose 1-phosphate. EC 2.7.7.9.
A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.
A non-pathogenic species of LACTOCOCCUS found in DAIRY PRODUCTS and responsible for the souring of MILK and the production of LACTIC ACID.
A pentose active in biological systems usually in its D-form.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Phlorhizin is a non-transportable glucose analog that inhibits the sodium-glucose cotransporter 1 (SGLT1) and aldohexose transporter (GLUT2), leading to reduced intestinal absorption and increased renal excretion of glucose, which is used in research to study glucose transport and diabetes-related processes.
Glycosphingolipids containing N-acetylglucosamine (paragloboside) or N-acetylgalactosamine (globoside). Globoside is the P antigen on erythrocytes and paragloboside is an intermediate in the biosynthesis of erythrocyte blood group ABH and P 1 glycosphingolipid antigens. The accumulation of globoside in tissue, due to a defect in hexosaminidases A and B, is the cause of Sandhoff disease.
Fractionation of a vaporized sample as a consequence of partition between a mobile gaseous phase and a stationary phase held in a column. Two types are gas-solid chromatography, where the fixed phase is a solid, and gas-liquid, in which the stationary phase is a nonvolatile liquid supported on an inert solid matrix.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A C-type lectin that is a cell surface receptor for ASIALOGLYCOPROTEINS. It is found primarily in the LIVER where it mediates the endocytosis of serum glycoproteins.
Monosaccharide transport proteins that function as active symporters. They utilize SODIUM or HYDROGEN IONS to transport GLUCOSE across CELL MEMBRANES.
Polysaccharides composed of repeating galactose units. They can consist of branched or unbranched chains in any linkages.
The sum of the weight of all the atoms in a molecule.
A genus of leguminous shrubs or trees, mainly tropical, yielding useful compounds such as ALKALOIDS and PLANT LECTINS.
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
An ascomycetous yeast of the fungal family Saccharomycetaceae, order SACCHAROMYCETALES.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Methylglycosides are glycosides with a methanol group (CH3-) replacing the hydrogen atom on the glycosidic oxygen, which can be found in various natural sources and have potential applications as sweetening agents or in pharmaceuticals.
Neutral glycosphingolipids that contain a monosaccharide, normally glucose or galactose, in 1-ortho-beta-glycosidic linkage with the primary alcohol of an N-acyl sphingoid (ceramide). In plants the monosaccharide is normally glucose and the sphingoid usually phytosphingosine. In animals, the monosaccharide is usually galactose, though this may vary with the tissue and the sphingoid is usually sphingosine or dihydrosphingosine. (From Oxford Dictionary of Biochemistry and Molecular Biology, 1st ed)
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
A subclass of ACIDIC GLYCOSPHINGOLIPIDS. They contain one or more sialic acid (N-ACETYLNEURAMINIC ACID) residues. Using the Svennerholm system of abbrevations, gangliosides are designated G for ganglioside, plus subscript M, D, or T for mono-, di-, or trisialo, respectively, the subscript letter being followed by a subscript arabic numeral to indicated sequence of migration in thin-layer chromatograms. (From Oxford Dictionary of Biochemistry and Molecular Biology, 1997)
Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.
The A protein of the lactose synthase complex. In the presence of the B protein (LACTALBUMIN) specificity is changed from N-acetylglucosamine to glucose. EC 2.4.1.90.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A group of enzymes with the general formula CMP-N-acetylneuraminate:acceptor N-acetylneuraminyl transferase. They catalyze the transfer of N-acetylneuraminic acid from CMP-N-acetylneuraminic acid to an acceptor, which is usually the terminal sugar residue of an oligosaccharide, a glycoprotein, or a glycolipid. EC 2.4.99.-.
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.

Gangliosides of human kidney. (1/3083)

Five gangliosides isolated from human kidney have been characterized. The two main fractions were shown to be typical extraneural gangliosides in having lactose as their neutral carbohydrate moiety. Their structures were identified as: AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-8)AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer. The two main hexosamine-containing gangliosides are structurally related to human blood group substances of glycosphingolipid nature. The following structures are postulated: AcNeu(alpha2-3)Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1) Cer. The third hexosamine-containing ganglioside belongs to a different series of glycolipids and was shown to have the structure of a major ganglioside of human brain: AcNeu(alpha2-3)Gal(beta1-3)GalNAc(beta1-4)[AcNeu(alpha2-3)]Gal(beta1-4)Glc(beta1- 1)Cer. The fatty acid structure of different gangliosides was shown to resemble that of neutral glycolipids of human kidney with the nonhydroxy acids C16:0, C22:0, and C24:0 as major components.  (+info)

Missense mutations in SGLT1 cause glucose-galactose malabsorption by trafficking defects. (2/3083)

Glucose-galactose malabsorption (GGM) is an autosomal recessive disorder caused by defects in the Na+/glucose cotransporter (SGLT1). Neonates present with severe diarrhea while on any diet containing glucose and/or galactose [1]. This study focuses on a patient of Swiss and Dominican descent. All 15 exons of SGLT1 were screened using single stranded conformational polymorphism analyses, and aberrant PCR products were sequenced. Two missense mutations, Gly318Arg and Ala468Val, were identified. SGLT1 mutants were expressed in Xenopus laevis oocytes for radiotracer uptake, electrophysiological experiments, and Western blotting. Uptakes of [14C]alpha-methyl-d-glucoside by the mutants were 5% or less than that of wild-type. Two-electrode voltage-clamp experiments confirmed the transport defects, as no noticeable sugar-induced current could be elicited from either mutant [2]. Western blots of cell protein showed levels of each SGLT1 mutant protein comparable to that of wild-type, and that both were core-glycosylated. Presteady-state current measurements indicated an absence of SGLT1 in the plasma membrane. We suggest that the compound heterozygote missense mutations G318R and A468V lead to GGM in this patient by defective trafficking of mutant proteins from the endoplasmic reticulum to the plasma membrane.  (+info)

Carbohydrate on human factor VIII/von Willebrand factor. Impairment of function by removal of specific galactose residues. (3/3083)

Human factor VIII/von Willebrand factor protein containing 120 +/- 12 nmol of sialic acid and 135 +/- 13 nmol of galactose/mg of protein was digested with neuraminidase. The affinity of native factor VIII/von Willebrand factor and its asialo form for the hepatic lectin that specifically binds asialoglycoproteins was assessed from in vitro binding experiments. Native factor VIII/von Willebrand factor exhibited negligible affinity while binding of the asialo derivative was comparable to that observed for asialo-alpha1-acid glycoprotein. Incubation of asialo-factor VIII/von Willebrand factor with Streptococcus pneumoniae beta-galactosidase removed only 62% of the galactose but abolished binding to the purified hepatic lectin. When the asialo derivative was incubated with purified beta-D-galactoside alpha2 leads to 6 sialyltransferase and CMP-[14C]NeuAc, only 61% of the galactose incorporated [14C]NeuAc. From the known specificites of these enzymes, it is concluded that galactose residues important in lectin binding are present in a terminal Gal/beta1 leads to 4GlcNAc sequence on asialo-factor VIII/von Willebrand factor. The relative ristocetin-induced platelet aggregating activity of native, asialo-, and agalacto-factor VIII/von Willebrand factor was 100:38:12, respectively, while procoagulant activity was 100:100:103.  (+info)

Stimulation of collagen galactosyltransferase and glucosyltransferase activities by lysophosphatidylcholine. (4/3083)

Lysophosphatidylcholine stimulated the activities of collagen galactosyl- and glucosyl-transferases in chick-embryo extract and its particulate fractions in vitro, whereas essentially no stimulation was noted in the high-speed supernatant, where the enzymes are soluble and membrane-free. The stimulatory effect of lysophosphatidylcholine was masked by 0.1% Triton X-100. In kinetic experiments lysophosphatidylcholine raised the maximum velocities with respect to the substrates and co-substrates, whereas no changes were observed in the apparant Km values. Phospholipase A preincubation of the chick-embryo extract resulted in stimulation of both transferase activities, probably gy generating lysophosphatides from endogenous phospholipids. No stimulation by lysophosphatidylcholine was found when tested with 500-fold-purified glycosyltransferase. The results suggest that collagen glycosyltransferases must be associated with the membrane structures of the cell in order to be stimulated by lysophosphatidylcholine. Lysophosphatidylcholine could have some regulatory significance in vivo, since its concentration in the cell is comparable with that which produced marked stimulation in vitro.  (+info)

Oligomycin induces a decrease in the cellular content of a pathogenic mutation in the human mitochondrial ATPase 6 gene. (5/3083)

A T --> G mutation at position 8993 in human mitochondrial DNA is associated with the syndrome neuropathy, ataxia, and retinitis pigmentosa and with a maternally inherited form of Leigh's syndrome. The mutation substitutes an arginine for a leucine at amino acid position 156 in ATPase 6, a component of the F0 portion of the mitochondrial ATP synthase complex. Fibroblasts harboring high levels of the T8993G mutation have decreased ATP synthesis activity, but do not display any growth defect under standard culture conditions. Combining the notions that cells with respiratory chain defects grow poorly in medium containing galactose as the major carbon source, and that resistance to oligomycin, a mitochondrial inhibitor, is associated with mutations in the ATPase 6 gene in the same transmembrane domain where the T8993G amino acid substitution is located, we created selective culture conditions using galactose and oligomycin that elicited a pathological phenotype in T8993G cells and that allowed for the rapid selection of wild-type over T8993G mutant cells. We then generated cytoplasmic hybrid clones containing heteroplasmic levels of the T8993G mutation, and showed that selection in galactose-oligomycin caused a significant increase in the fraction of wild-type molecules (from 16 to 28%) in these cells.  (+info)

Quantitative determination of N-acetylglucosamine residues at the non-reducing ends of peptidoglycan chains by enzymic attachment of [14C]-D-galactose. (6/3083)

The ability of human milk galactosyltransferase to attach D-galactose residues quantitatively to the C-4 of N-acetylglucosamine moieties at the ends of oligosaccharides has been utilized for the specific labeling and quantitative determination of the chain length of the glycan moiety of the bacterial cell wall. The average polysaccharide chain length of the soluble, uncrosslinked peptidoglycan secreted by Micrococcus luteus cells on incubation with penicillin G was studied with this technique and found to be approximately 70 hexosamines long. Furthermore, the peptidoglycan chain length of Escherichia coli sacculi of different cell shapes and dimensions was determined both in rod-shaped cells and in filaments induced by temperature shift of a division mutant or by addition of cephalexin or nalidixic acid. The average chain length found in most of these sacculi was between 70 and 100 hexosamines long. Small spherical 'mini' cells had chain lengths similar to those of the isogenic rod-like cells.  (+info)

A unique primary structure, cDNA cloning and function of a galactose-specific lectin from ascidian plasma. (7/3083)

The complete amino acid sequence of a galactose-specific lectin from the plasma of the ascidian Halocynthia roretzi has been determined by sequential Edman degradation analysis of peptide fragments derived by proteolytic fragmentation and chemical cleavage of the reductive S-pyridylethylated lectin. Peptide fragments were separated by reverse-phase HPLC. The N-terminal and C-terminal amino acid sequences were determined by Edman degradation and enzymatic digestion. The H. roretzi plasma lectin is a single-chain protein consisting of 327 amino acids and four disulfide bonds, one of which was found to be cross-linked intramolecularly. A comparison of the amino acid sequence of the H. roretzi plasma lectin with the sequences of other proteins reveals that the H. roretzi lectin has a structure consisting of a twice-repeated sequence, a fibrinogen-related sequence and a C-type lectin-homologous sequence. The above amino acid sequence was verified by cDNA cloning of this lectin. Three cDNA clones that have single ORFs encoding the lectin precursor were isolated from an H. roretzi hepatopancreas cDNA library. The deduced amino acid sequences in the three cDNA clones contain the same sequence of the mature lectin molecule and the same putative signal sequence. In addition, it was demonstrated that this lectin can enhance phagocytosis by H. roretzi hemocytes. Thus, the plasma lectin is constructed into an oligomer structure via intermolecular disulfide bonds and plays a role in the biological defense of H. roretzi as a defense molecule.  (+info)

Orotate decreases the inhibitory effect of ethanol on galactose elimination in the perfused rat liver. (8/3083)

1. The galactose-elimination rate in perfused livers from starved rats was decreased in the presence of ethanol (2-28mM) to one-third of the control values. Orotate injections partly reversed the effect of ethanol, so that the galactose-elimination rate was about two-thirds of the control values. Orotate alone had no effect on the galactose-elimination rate. 2. Ethanol increased [galactose 1-phosphate] and [UDP-galactose], and decreased (UDP-glucose] and [UTP], both with and without orotate. Orotate increased [UTP], [UDP-galactose], both with and without ethanol. The increase of [galactose 1-phosphate] in the presence of ethanol was inhibited by orotate. Orotate alone had no appreciable effect on [galactose 1-phosphate]. 3. Both the effect of ethanol and that of orotate on the galactose-elimination rate can be accounted for by assuming inhibition of galactokinase by galactose 1-phosphate with Ki about 0.2mM, the inhibition being either non-competitive or uncompetitive. 4. The primary effect of ethanol seems to be inhibition of UDP-glucose epimerase (EC 5.1.3.2), followed by accumulation of UDP-galactose, trapping of UDP-glucose and increase of [galactose 1-phosphate]. Orotate decreased the effect of ethanol, probably by increasing [UDP-glucose].  (+info)

Galactose is a simple sugar or monosaccharide that is a constituent of lactose, the disaccharide found in milk and dairy products. It's structurally similar to glucose but with a different chemical structure, and it plays a crucial role in various biological processes.

Galactose can be metabolized in the body through the action of enzymes such as galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-galactose 4'-epimerase. Inherited deficiencies in these enzymes can lead to metabolic disorders like galactosemia, which can cause serious health issues if not diagnosed and treated promptly.

In summary, Galactose is a simple sugar that plays an essential role in lactose metabolism and other biological processes.

Galactose oxidase is an enzyme with the systematic name D-galactose:oxygen oxidoreductase. It is found in certain fungi and bacteria, and it catalyzes the following reaction:

D-galactose + O2 -> D-galacto-hexodialdose + H2O2

In this reaction, the enzyme oxidizes the hydroxyl group (-OH) on the sixth carbon atom of D-galactose to an aldehyde group (-CHO), forming D-galacto-hexodialdose. At the same time, it reduces molecular oxygen (O2) to hydrogen peroxide (H2O2).

Galactose oxidase is a copper-containing enzyme and requires the cofactor molybdenum for its activity. It has potential applications in various industrial processes, such as the production of D-galacto-hexodialdose and other sugar derivatives, as well as in biosensors for detecting glucose levels in biological samples.

Galactose dehydrogenases (GDH) are a group of enzymes that play a role in the metabolism of galactose, a simple sugar that is a component of lactose and other complex carbohydrates. These enzymes catalyze the oxidation of galactose to galactonate, using NAD+ as an electron acceptor. This reaction is part of the pathway that converts galactose to glucose in the body.

There are several different isoforms of galactose dehydrogenases found in various tissues and organisms, including:

1. GDH1 (also known as GALT): This is the primary form of galactose dehydrogenase found in humans and other mammals. It is located in the cytosol of cells and is responsible for the majority of galactose metabolism. Mutations in this gene can lead to a genetic disorder called classic galactosemia, which is characterized by an inability to metabolize galactose properly.
2. GDH2 (also known as G Aldo): This form of galactose dehydrogenase is found in the endoplasmic reticulum and is involved in the quality control of glycoproteins. It catalyzes the reverse reaction, reducing galactonate to galactose.
3. GDH3 (also known as G AldoX): This form of galactose dehydrogenase is found in the mitochondria and is involved in the metabolism of ascorbic acid (vitamin C). It also catalyzes the reverse reaction, reducing galactonate to galactose.
4. BGDH: This form of galactose dehydrogenase is found in bacteria and some plants. It is involved in the metabolism of both galactose and glucose.

Deficiencies or mutations in these enzymes can lead to various metabolic disorders, including galactosemia, which can cause a range of symptoms such as cataracts, developmental delays, and liver damage.

I'm sorry for any confusion, but "galactosephosphates" is not a widely recognized or established term in medicine or biochemistry. It seems that this term may be a combination of "galactose," which is a simple sugar, and "phosphate," which is a common ion found in biological systems. However, without more context, it's difficult to provide an accurate medical definition for this term.

Galactose is a monosaccharide that is metabolized in the body through the Leloir pathway, and defects in this pathway can lead to genetic disorders such as galactosemia. Phosphates are often found in biological molecules, including nucleic acids (DNA and RNA) and certain sugars (like glucose-1-phosphate).

Without further context or information about how "galactosephosphates" is being used, I would be cautious about assuming that it refers to a specific medical concept or condition.

Galactosemia is a rare metabolic disorder that affects the body's ability to metabolize the simple sugar galactose, which is found in milk and other dairy products. It is caused by deficiency or complete absence of one of the three enzymes needed to convert galactose into glucose:

1. Galactokinase (GALK) deficiency - also known as Galactokinase galactosemia, is a milder form of the disorder.
2. Galactose-1-phosphate uridylyltransferase (GALT) deficiency - the most common and severe form of classic galactosemia.
3. Galactose epimerase (GALE) deficiency - also known as Epimerase deficiency galactosemia, is a rare and milder form of the disorder.

The most severe form of the disorder, GALT deficiency, can lead to serious health problems such as cataracts, liver damage, mental retardation, and sepsis if left untreated. Treatment typically involves removing galactose from the diet, which requires avoiding all milk and dairy products. Early diagnosis and treatment are crucial for improving outcomes in individuals with galactosemia.

Uridine Diphosphate Galactose (UDP-galactose) is a nucleotide sugar that plays a crucial role in the biosynthesis of glycans, proteoglycans, and glycolipids. It is formed from uridine diphosphate glucose (UDP-glucose) through the action of the enzyme UDP-glucose 4'-epimerase.

In the body, UDP-galactose serves as a galactosyl donor in various metabolic pathways, including lactose synthesis in the mammary gland and the addition of galactose residues to proteoglycans and glycoproteins in the Golgi apparatus. Defects in the metabolism of UDP-galactose have been linked to several genetic disorders, such as galactosemia, which can result in serious health complications if left untreated.

UDP-glucose 4-epimerase (UGE) is an enzyme that catalyzes the reversible interconversion of UDP-galactose and UDP-glucose, two important nucleotide sugars involved in carbohydrate metabolism. This enzyme plays a crucial role in maintaining the balance between these two molecules, which are essential for the synthesis of various glycoconjugates, such as glycoproteins and proteoglycans. UGE is widely distributed in nature and has been identified in various organisms, including humans. In humans, deficiency or mutations in this enzyme can lead to a rare genetic disorder known as galactosemia, which is characterized by an impaired ability to metabolize the sugar galactose, resulting in several health issues.

Galactokinase is a medical/biochemical term that refers to the enzyme responsible for the first step in the metabolic pathway of galactose, a simple sugar or monosaccharide. This enzyme catalyzes the phosphorylation of D-galactose to form D-galactose 1-phosphate, using ATP as the phosphate donor.

Galactokinase is a crucial enzyme in the metabolism of lactose and other galactose-containing carbohydrates. Deficiency or mutation in this enzyme can lead to a genetic disorder called Galactokinase Deficiency, which results in the accumulation of galactose and its derivatives in body tissues, potentially causing cataracts and other symptoms associated with galactosemia.

UTP-hexose-1-phosphate uridylyltransferase is an enzyme that catalyzes the transfer of a uridine monophosphate (UMP) group from a uridine triphosphate (UTP) molecule to a hexose-1-phosphate molecule, forming a UDP-hexose molecule. This reaction is an essential step in the biosynthesis of various glycosylated compounds, including glycoproteins and polysaccharides.

The systematic name for this enzyme is UTP:alpha-D-hexose-1-phosphate uridylyltransferase. It is also known as UDP-glucose pyrophosphorylase, which is a more specific name that refers to the formation of UDP-glucose from glucose-1-phosphate and UTP.

The enzyme plays a crucial role in carbohydrate metabolism and has been implicated in several diseases, including diabetes and cancer. Inhibitors of this enzyme have been explored as potential therapeutic agents for the treatment of these conditions.

Galactitol is not a medical term per se, but it is a term used in biochemistry and medicine. Galactitol, also known as dulcitol, is a sugar alcohol that is formed in the body when an enzyme called galactose-1-phosphate uridylyltransferase (GALT) is missing or not functioning properly.

This enzyme deficiency can lead to a genetic disorder called galactosemia, which affects the body's ability to metabolize the sugar galactose, found in milk and other dairy products. When an individual with galactosemia consumes foods containing galactose, the galactose cannot be properly broken down and converted into glucose for energy. Instead, it gets converted into galactitol, which can accumulate in various tissues of the body, including the eyes, kidneys, and nervous system.

The accumulation of galactitol can cause a range of symptoms, such as cataracts, developmental delays, speech problems, and mental impairment. Therefore, individuals with galactosemia must follow a strict diet that avoids foods containing galactose to prevent the buildup of galactitol and its associated health complications.

Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).

Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.

Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.

Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.

Fucose is a type of sugar molecule that is often found in complex carbohydrates known as glycans, which are attached to many proteins and lipids in the body. It is a hexose sugar, meaning it contains six carbon atoms, and is a type of L-sugar, which means that it rotates plane-polarized light in a counterclockwise direction.

Fucose is often found at the ends of glycan chains and plays important roles in various biological processes, including cell recognition, signaling, and interaction. It is also a component of some blood group antigens and is involved in the development and function of the immune system. Abnormalities in fucosylation (the addition of fucose to glycans) have been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Lactose is a disaccharide, a type of sugar, that is naturally found in milk and dairy products. It is made up of two simple sugars, glucose and galactose, linked together. In order for the body to absorb and use lactose, it must be broken down into these simpler sugars by an enzyme called lactase, which is produced in the lining of the small intestine.

People who have a deficiency of lactase are unable to fully digest lactose, leading to symptoms such as bloating, diarrhea, and abdominal cramps, a condition known as lactose intolerance.

Monosaccharides are simple sugars that cannot be broken down into simpler units by hydrolysis. They are the most basic unit of carbohydrates and are often referred to as "simple sugars." Monosaccharides typically contain three to seven atoms of carbon, but the most common monosaccharides contain five or six carbon atoms.

The general formula for a monosaccharide is (CH2O)n, where n is the number of carbon atoms in the molecule. The majority of monosaccharides have a carbonyl group (aldehyde or ketone) and multiple hydroxyl groups. These functional groups give monosaccharides their characteristic sweet taste and chemical properties.

The most common monosaccharides include glucose, fructose, and galactose, all of which contain six carbon atoms and are known as hexoses. Other important monosaccharides include pentoses (five-carbon sugars) such as ribose and deoxyribose, which play crucial roles in the structure and function of nucleic acids (DNA and RNA).

Monosaccharides can exist in various forms, including linear and cyclic structures. In aqueous solutions, monosaccharides often form cyclic structures through a reaction between the carbonyl group and a hydroxyl group, creating a hemiacetal or hemiketal linkage. These cyclic structures can adopt different conformations, known as anomers, depending on the orientation of the hydroxyl group attached to the anomeric carbon atom.

Monosaccharides serve as essential building blocks for complex carbohydrates, such as disaccharides (e.g., sucrose, lactose, and maltose) and polysaccharides (e.g., starch, cellulose, and glycogen). They also participate in various biological processes, including energy metabolism, cell recognition, and protein glycosylation.

Galactosyltransferases are a group of enzymes that play a crucial role in the biosynthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of many cell types. These enzymes catalyze the transfer of galactose, a type of sugar, to another molecule, such as another sugar or a lipid, to form a glycosidic bond.

Galactosyltransferases are classified based on the type of donor substrate they use and the type of acceptor substrate they act upon. For example, some galactosyltransferases use UDP-galactose as a donor substrate and transfer galactose to an N-acetylglucosamine (GlcNAc) residue on a protein or lipid, forming a lactosamine unit. Others may use different donor and acceptor substrates to form different types of glycosidic linkages.

These enzymes are involved in various biological processes, including cell recognition, signaling, and adhesion. Abnormalities in the activity of galactosyltransferases have been implicated in several diseases, such as congenital disorders of glycosylation, cancer, and inflammatory conditions. Therefore, understanding the function and regulation of these enzymes is important for developing potential therapeutic strategies for these diseases.

Hexoses are simple sugars (monosaccharides) that contain six carbon atoms. The most common hexoses include glucose, fructose, and galactose. These sugars play important roles in various biological processes, such as serving as energy sources or forming complex carbohydrates like starch and cellulose. Hexoses are essential for the structure and function of living organisms, including humans.

Acetylgalactosamine (also known as N-acetyl-D-galactosamine or GalNAc) is a type of sugar molecule called a hexosamine that is commonly found in glycoproteins and proteoglycans, which are complex carbohydrates that are attached to proteins and lipids. It plays an important role in various biological processes, including cell-cell recognition, signal transduction, and protein folding.

In the context of medical research and biochemistry, Acetylgalactosamine is often used as a building block for synthesizing glycoconjugates, which are molecules that consist of a carbohydrate attached to a protein or lipid. These molecules play important roles in many biological processes, including cell-cell recognition, signaling, and immune response.

Acetylgalactosamine is also used as a target for enzymes called glycosyltransferases, which add sugar molecules to proteins and lipids. In particular, Acetylgalactosamine is the acceptor substrate for a class of glycosyltransferases known as galactosyltransferases, which add galactose molecules to Acetylgalactosamine-containing structures.

Defects in the metabolism of Acetylgalactosamine have been linked to various genetic disorders, including Schindler disease and Kanzaki disease, which are characterized by neurological symptoms and abnormal accumulation of glycoproteins in various tissues.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

Mannose is a simple sugar (monosaccharide) that is similar in structure to glucose. It is a hexose, meaning it contains six carbon atoms. Mannose is a stereoisomer of glucose, meaning it has the same chemical formula but a different structural arrangement of its atoms.

Mannose is not as commonly found in foods as other simple sugars, but it can be found in some fruits, such as cranberries, blueberries, and peaches, as well as in certain vegetables, like sweet potatoes and turnips. It is also found in some dietary fibers, such as those found in beans and whole grains.

In the body, mannose can be metabolized and used for energy, but it is also an important component of various glycoproteins and glycolipids, which are molecules that play critical roles in many biological processes, including cell recognition, signaling, and adhesion.

Mannose has been studied as a potential therapeutic agent for various medical conditions, including urinary tract infections (UTIs), because it can inhibit the attachment of certain bacteria to the cells lining the urinary tract. Additionally, mannose-binding lectins have been investigated for their potential role in the immune response to viral and bacterial infections.

A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.

For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.

Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.

UDP-glucose-hexose-1-phosphate uridylyltransferase is an enzyme that plays a role in the metabolism of carbohydrates. The systematic name for this enzyme is UDP-glucose:alpha-D-hexose-1-phosphate uridylyltransferase.

This enzyme catalyzes the following reaction:
UDP-glucose + alpha-D-hexose 1-phosphate glucose 1-phosphate + UDP-alpha-D-hexose

In simpler terms, this enzyme helps to transfer a uridylyl group (UDP) from UDP-glucose to another hexose sugar that is attached to a phosphate group. This reaction allows for the interconversion of different sugars in the cell and plays a role in various metabolic pathways, including the synthesis of glycogen and other complex carbohydrates.

Deficiencies or mutations in this enzyme can lead to various genetic disorders, such as congenital disorder of glycosylation type IIb (CDGIIb) and polycystic kidney disease.

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

Carbohydrate conformation refers to the three-dimensional shape and structure of a carbohydrate molecule. Carbohydrates, also known as sugars, can exist in various conformational states, which are determined by the rotation of their component bonds and the spatial arrangement of their functional groups.

The conformation of a carbohydrate molecule can have significant implications for its biological activity and recognition by other molecules, such as enzymes or antibodies. Factors that can influence carbohydrate conformation include the presence of intramolecular hydrogen bonds, steric effects, and intermolecular interactions with solvent molecules or other solutes.

In some cases, the conformation of a carbohydrate may be stabilized by the formation of cyclic structures, in which the hydroxyl group at one end of the molecule forms a covalent bond with the carbonyl carbon at the other end, creating a ring structure. The most common cyclic carbohydrates are monosaccharides, such as glucose and fructose, which can exist in various conformational isomers known as anomers.

Understanding the conformation of carbohydrate molecules is important for elucidating their biological functions and developing strategies for targeting them with drugs or other therapeutic agents.

Galactosidases are a group of enzymes that catalyze the hydrolysis of galactose-containing sugars, specifically at the beta-glycosidic bond. There are several types of galactosidases, including:

1. Beta-galactosidase: This is the most well-known type of galactosidase and it catalyzes the hydrolysis of lactose into glucose and galactose. It has important roles in various biological processes, such as lactose metabolism in animals and cell wall biosynthesis in plants.
2. Alpha-galactosidase: This enzyme catalyzes the hydrolysis of alpha-galactosides, which are found in certain plant-derived foods like legumes. A deficiency in this enzyme can lead to a genetic disorder called Fabry disease.
3. N-acetyl-beta-glucosaminidase: This enzyme is also known as hexosaminidase and it catalyzes the hydrolysis of N-acetyl-beta-D-glucosamine residues from glycoproteins, glycolipids, and other complex carbohydrates.

Galactosidases are widely used in various industrial applications, such as food processing, biotechnology, and biofuel production. They also have potential therapeutic uses, such as in the treatment of lysosomal storage disorders like Fabry disease.

Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.

The most common disaccharides include:

* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.

Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.

Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.

I'm sorry for any confusion, but "Methylgalactosides" is not a recognized term in medical or biological nomenclature. It appears that the term may be a combination of "methyl," a common chemical modification, and "galactosides," which are compounds containing galactose, a type of sugar. However, without more context, it's difficult to provide an accurate definition or medical relevance.

If you meant a different term or need information on a related topic, please provide more details so I can give a more helpful response.

Carbohydrate epimerases are a group of enzymes that catalyze the interconversion of specific stereoisomers (epimers) of carbohydrates by the reversible oxidation and reduction of carbon atoms, usually at the fourth or fifth position. These enzymes play important roles in the biosynthesis and modification of various carbohydrate-containing molecules, such as glycoproteins, proteoglycans, and glycolipids, which are involved in numerous biological processes including cell recognition, signaling, and adhesion.

The reaction catalyzed by carbohydrate epimerases involves the transfer of a hydrogen atom and a proton between two adjacent carbon atoms, leading to the formation of new stereochemical configurations at these positions. This process can result in the conversion of one epimer into another, thereby expanding the structural diversity of carbohydrates and their derivatives.

Carbohydrate epimerases are classified based on the type of substrate they act upon and the specific stereochemical changes they induce. Some examples include UDP-glucose 4-epimerase, which interconverts UDP-glucose and UDP-galactose; UDP-N-acetylglucosamine 2-epimerase, which converts UDP-N-acetylglucosamine to UDP-N-acetylmannosamine; and GDP-fucose synthase, which catalyzes the conversion of GDP-mannose to GDP-fucose.

Understanding the function and regulation of carbohydrate epimerases is crucial for elucidating their roles in various biological processes and developing strategies for targeting them in therapeutic interventions.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

Phosphoglucomutase (PGM) is an enzyme involved in carbohydrate metabolism, specifically in the glycolysis and gluconeogenesis pathways. It catalyzes the reversible conversion of glucose-6-phosphate (G6P) to glucose-1-phosphate (G1P), and vice versa.

In humans, there are three isoforms of phosphoglucomutase: PGM1, PGM2, and PGM3, which are encoded by different genes. These isoforms have distinct tissue distributions and functions. For example, PGM1 is widely expressed in various tissues, while PGM2 is primarily found in the brain and testis.

Phosphoglucomutase plays a crucial role in maintaining glucose homeostasis by interconverting G6P and G1P, which are precursors for glycogen synthesis and degradation, respectively. Deficiencies in phosphoglucomutase can lead to metabolic disorders such as muscle phosphorylase deficiency (McArdle disease) or type IV glycogen storage disease (GSD IV).

Glucosamine is a natural compound found in the body, primarily in the fluid around joints. It is a building block of cartilage, which is the tissue that cushions bones and allows for smooth joint movement. Glucosamine can also be produced in a laboratory and is commonly sold as a dietary supplement.

Medical definitions of glucosamine describe it as a type of amino sugar that plays a crucial role in the formation and maintenance of cartilage, ligaments, tendons, and other connective tissues. It is often used as a supplement to help manage osteoarthritis symptoms, such as pain, stiffness, and swelling in the joints, by potentially reducing inflammation and promoting cartilage repair.

There are different forms of glucosamine available, including glucosamine sulfate, glucosamine hydrochloride, and N-acetyl glucosamine. Glucosamine sulfate is the most commonly used form in supplements and has been studied more extensively than other forms. While some research suggests that glucosamine may provide modest benefits for osteoarthritis symptoms, its effectiveness remains a topic of ongoing debate among medical professionals.

Paper chromatography is a type of chromatography technique that involves the separation and analysis of mixtures based on their components' ability to migrate differently upon capillary action on a paper medium. This simple and cost-effective method utilizes a paper, typically made of cellulose, as the stationary phase. The sample mixture is applied as a small spot near one end of the paper, and then the other end is dipped into a developing solvent or a mixture of solvents (mobile phase) in a shallow container.

As the mobile phase moves up the paper by capillary action, components within the sample mixture separate based on their partition coefficients between the stationary and mobile phases. The partition coefficient describes how much a component prefers to be in either the stationary or mobile phase. Components with higher partition coefficients in the mobile phase will move faster and further than those with lower partition coefficients.

Once separation is complete, the paper is dried and can be visualized under ultraviolet light or by using chemical reagents specific for the components of interest. The distance each component travels from the origin (point of application) and its corresponding solvent front position are measured, allowing for the calculation of Rf values (retardation factors). Rf is a dimensionless quantity calculated as the ratio of the distance traveled by the component to the distance traveled by the solvent front.

Rf = (distance traveled by component) / (distance traveled by solvent front)

Paper chromatography has been widely used in various applications, such as:

1. Identification and purity analysis of chemical compounds in pharmaceuticals, forensics, and research laboratories.
2. Separation and detection of amino acids, sugars, and other biomolecules in biological samples.
3. Educational purposes to demonstrate the principles of chromatography and separation techniques.

Despite its limitations, such as lower resolution compared to high-performance liquid chromatography (HPLC) and less compatibility with volatile or nonpolar compounds, paper chromatography remains a valuable tool for quick, qualitative analysis in various fields.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Glycopeptides are a class of antibiotics that are characterized by their complex chemical structure, which includes both peptide and carbohydrate components. These antibiotics are produced naturally by certain types of bacteria and are effective against a range of Gram-positive bacterial infections, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE).

The glycopeptide antibiotics work by binding to the bacterial cell wall precursor, preventing the cross-linking of peptidoglycan chains that is necessary for the formation of a strong and rigid cell wall. This leads to the death of the bacteria.

Examples of glycopeptides include vancomycin, teicoplanin, and dalbavancin. While these antibiotics have been used successfully for many years, their use is often limited due to concerns about the emergence of resistance and potential toxicity.

Amino sugars, also known as glycosamine or hexosamines, are sugar molecules that contain a nitrogen atom as part of their structure. The most common amino sugars found in nature are glucosamine and galactosamine, which are derived from the hexose sugars glucose and galactose, respectively.

Glucosamine is an essential component of the structural polysaccharide chitin, which is found in the exoskeletons of arthropods such as crustaceans and insects, as well as in the cell walls of fungi. It is also a precursor to the glycosaminoglycans (GAGs), which are long, unbranched polysaccharides that are important components of the extracellular matrix in animals.

Galactosamine, on the other hand, is a component of some GAGs and is also found in bacterial cell walls. It is used in the synthesis of heparin and heparan sulfate, which are important anticoagulant molecules.

Amino sugars play a critical role in many biological processes, including cell signaling, inflammation, and immune response. They have also been studied for their potential therapeutic uses in the treatment of various diseases, such as osteoarthritis and cancer.

Sialic acids are a family of nine-carbon sugars that are commonly found on the outermost surface of many cell types, particularly on the glycoconjugates of mucins in various secretions and on the glycoproteins and glycolipids of cell membranes. They play important roles in a variety of biological processes, including cell recognition, immune response, and viral and bacterial infectivity. Sialic acids can exist in different forms, with N-acetylneuraminic acid being the most common one in humans.

Glycolipids are a type of lipid (fat) molecule that contain one or more sugar molecules attached to them. They are important components of cell membranes, where they play a role in cell recognition and signaling. Glycolipids are also found on the surface of some viruses and bacteria, where they can be recognized by the immune system as foreign invaders.

There are several different types of glycolipids, including cerebrosides, gangliosides, and globosides. These molecules differ in the number and type of sugar molecules they contain, as well as the structure of their lipid tails. Glycolipids are synthesized in the endoplasmic reticulum and Golgi apparatus of cells, and they are transported to the cell membrane through vesicles.

Abnormalities in glycolipid metabolism or structure have been implicated in a number of diseases, including certain types of cancer, neurological disorders, and autoimmune diseases. For example, mutations in genes involved in the synthesis of glycolipids can lead to conditions such as Tay-Sachs disease and Gaucher's disease, which are characterized by the accumulation of abnormal glycolipids in cells.

Uridine diphosphate sugars (UDP-sugars) are nucleotide sugars that play a crucial role in the biosynthesis of glycans, which are complex carbohydrates found on the surface of many cell types. UDP-sugars consist of a uridine diphosphate molecule linked to a sugar moiety, such as glucose, galactose, or xylose. These molecules serve as activated donor substrates for glycosyltransferases, enzymes that catalyze the transfer of sugar residues to acceptor molecules, including proteins and other carbohydrates. UDP-sugars are essential for various biological processes, such as cell recognition, signaling, and protein folding. Dysregulation of UDP-sugar metabolism has been implicated in several diseases, including cancer and congenital disorders of glycosylation.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Galactosides are compounds that contain a galactose molecule. Galactose is a monosaccharide, or simple sugar, that is similar in structure to glucose but has a different chemical formula (C~6~H~10~O~5~). It is found in nature and is a component of lactose, the primary sugar in milk.

Galactosides are formed when a galactose molecule is linked to another molecule through a glycosidic bond. This type of bond is formed between a hydroxyl group (-OH) on the galactose molecule and a functional group on the other molecule. Galactosides can be found in various substances, including some plants and microorganisms, as well as in certain medications and medical supplements.

One common example of a galactoside is lactose, which is a disaccharide consisting of a glucose molecule linked to a galactose molecule through a glycosidic bond. Lactose is the primary sugar found in milk and dairy products, and it is broken down into its component monosaccharides (glucose and galactose) by an enzyme called lactase during digestion.

Other examples of galactosides include various glycoproteins, which are proteins that have one or more galactose molecules attached to them. These types of compounds play important roles in the body, including in cell-cell recognition and communication, as well as in the immune response.

Borohydrides are a class of chemical compounds that contain boron and hydrogen ions (H-). The most common borohydride is sodium borohydride (NaBH4), which is a white, solid compound often used in chemistry as a reducing agent. Borohydrides are known for their ability to donate hydride ions (H:-) in chemical reactions, making them useful for reducing various organic and inorganic compounds. Other borohydrides include lithium borohydride (LiBH4), potassium borohydride (KBH4), and calcium borohydride (Ca(BH4)2).

Plant lectins are proteins or glycoproteins that are abundantly found in various plant parts such as seeds, leaves, stems, and roots. They have the ability to bind specifically to carbohydrate structures present on cell membranes, known as glycoconjugates. This binding property of lectins is reversible and non-catalytic, meaning it does not involve any enzymatic activity.

Lectins play several roles in plants, including defense against predators, pathogens, and herbivores. They can agglutinate red blood cells, stimulate the immune system, and have been implicated in various biological processes such as cell growth, differentiation, and apoptosis (programmed cell death). Some lectins also exhibit mitogenic activity, which means they can stimulate the proliferation of certain types of cells.

In the medical field, plant lectins have gained attention due to their potential therapeutic applications. For instance, some lectins have been shown to possess anti-cancer properties and are being investigated as potential cancer treatments. However, it is important to note that some lectins can be toxic or allergenic to humans and animals, so they must be used with caution.

Acetylglucosamine is a type of sugar that is commonly found in the body and plays a crucial role in various biological processes. It is a key component of glycoproteins and proteoglycans, which are complex molecules made up of protein and carbohydrate components.

More specifically, acetylglucosamine is an amino sugar that is formed by the addition of an acetyl group to glucosamine. It can be further modified in the body through a process called acetylation, which involves the addition of additional acetyl groups.

Acetylglucosamine is important for maintaining the structure and function of various tissues in the body, including cartilage, tendons, and ligaments. It also plays a role in the immune system and has been studied as a potential therapeutic target for various diseases, including cancer and inflammatory conditions.

In summary, acetylglucosamine is a type of sugar that is involved in many important biological processes in the body, and has potential therapeutic applications in various diseases.

Asialoglycoproteins are glycoproteins that have lost their terminal sialic acid residues. In the body, these molecules are typically recognized and removed from circulation by hepatic lectins, such as the Ashwell-Morrell receptor, found on liver cells. This process is a part of the normal turnover and clearance of glycoproteins in the body.

Hexosamines are amino sugars that are formed by the substitution of an amino group (-NH2) for a hydroxyl group (-OH) in a hexose sugar. The most common hexosamine is N-acetylglucosamine (GlcNAc), which is derived from glucose. Other hexosamines include galactosamine, mannosamine, and fucosamine.

Hexosamines play important roles in various biological processes, including the formation of glycosaminoglycans, proteoglycans, and glycoproteins. These molecules are involved in many cellular functions, such as cell signaling, cell adhesion, and protein folding. Abnormalities in hexosamine metabolism have been implicated in several diseases, including diabetes, cancer, and neurodegenerative disorders.

Arabinose is a simple sugar or monosaccharide that is a stereoisomer of xylose. It is a pentose, meaning it contains five carbon atoms, and is classified as a hexahydroxyhexital because it has six hydroxyl (-OH) groups attached to the carbon atoms. Arabinose is found in various plant polysaccharides, such as hemicelluloses, gums, and pectic substances. It can also be found in some bacteria and yeasts, where it plays a role in their metabolism. In humans, arabinose is not an essential nutrient and must be metabolized by specific enzymes if consumed.

Glycosides are organic compounds that consist of a glycone (a sugar component) linked to a non-sugar component, known as an aglycone, via a glycosidic bond. They can be found in various plants, microorganisms, and some animals. Depending on the nature of the aglycone, glycosides can be classified into different types, such as anthraquinone glycosides, cardiac glycosides, and saponin glycosides.

These compounds have diverse biological activities and pharmacological effects. For instance:

* Cardiac glycosides, like digoxin and digitoxin, are used in the treatment of heart failure and certain cardiac arrhythmias due to their positive inotropic (contractility-enhancing) and negative chronotropic (heart rate-slowing) effects on the heart.
* Saponin glycosides have potent detergent properties and can cause hemolysis (rupture of red blood cells). They are used in various industries, including cosmetics and food processing, and have potential applications in drug delivery systems.
* Some glycosides, like amygdalin found in apricot kernels and bitter almonds, can release cyanide upon hydrolysis, making them potentially toxic.

It is important to note that while some glycosides have therapeutic uses, others can be harmful or even lethal if ingested or otherwise introduced into the body in large quantities.

Rhamnose is a naturally occurring sugar or monosaccharide, that is commonly found in various plants and some fruits. It is a type of deoxy sugar, which means it lacks one hydroxyl group (-OH) compared to a regular hexose sugar. Specifically, rhamnose has a hydrogen atom instead of a hydroxyl group at the 6-position of its structure.

Rhamnose is an essential component of various complex carbohydrates and glycoconjugates found in plant cell walls, such as pectins and glycoproteins. It also plays a role in bacterial cell wall biosynthesis and is used in the production of some antibiotics.

In medical contexts, rhamnose may be relevant to research on bacterial infections, plant-derived medicines, or the metabolism of certain sugars. However, it is not a commonly used term in clinical medicine.

Neuraminic acids, also known as sialic acids, are a family of nine-carbon sugars that are commonly found on the outermost layer of many cell surfaces in animals. They play important roles in various biological processes, such as cell recognition, immune response, and viral and bacterial infection. Neuraminic acids can exist in several forms, with N-acetylneuraminic acid (NANA) being the most common one in mammals. They are often found attached to other sugars to form complex carbohydrates called glycoconjugates, which are involved in many cellular functions and interactions.

Fetuins are a group of proteins that are produced by the liver and found in circulation in the blood. The most well-known fetuin, fetuin-A, is a 64 kDa glycoprotein that is synthesized in the liver and secreted into the bloodstream. Fetuin-A plays a role in several physiological processes, including inhibition of tissue calcification, regulation of insulin sensitivity, and modulation of immune responses.

Fetuin-B is another member of the fetuin family that shares some structural similarities with fetuin-A but has distinct functions. Fetuin-B is also produced by the liver and secreted into the bloodstream, where it plays a role in regulating lipid metabolism and insulin sensitivity.

It's worth noting that while both fetuins have been studied for their roles in various physiological processes, there is still much to be learned about their functions and regulation.

Glycosphingolipids are a type of complex lipid molecule found in animal cell membranes, particularly in the outer leaflet of the plasma membrane. They consist of a hydrophobic ceramide backbone, which is composed of sphingosine and fatty acids, linked to one or more hydrophilic sugar residues, such as glucose or galactose.

Glycosphingolipids can be further classified into two main groups: neutral glycosphingolipids (which include cerebrosides and gangliosides) and acidic glycosphingolipids (which are primarily gangliosides). Glycosphingolipids play important roles in various cellular processes, including cell recognition, signal transduction, and cell adhesion.

Abnormalities in the metabolism or structure of glycosphingolipids have been implicated in several diseases, such as lysosomal storage disorders (e.g., Gaucher's disease, Fabry's disease) and certain types of cancer (e.g., ganglioside-expressing neuroblastoma).

Galactosamine is not a medical condition but a chemical compound. Medically, it might be referred to in the context of certain medical tests or treatments. Here's the scientific definition:

Galactosamine is an amino sugar, a type of monosaccharide (simple sugar) that contains a functional amino group (-NH2) as well as a hydroxyl group (-OH). More specifically, galactosamine is a derivative of galactose, with the chemical formula C6H13NO5. It is an important component of many glycosaminoglycans (GAGs), which are complex carbohydrates found in animal tissues, particularly in connective tissue and cartilage.

In some medical applications, galactosamine has been used as a building block for the synthesis of GAG analogs or as a component of substrates for enzyme assays. It is also used in research to study various biological processes, such as cell growth and differentiation.

Periodic acid is not a medical term per se, but it is a chemical reagent that is used in some laboratory tests and staining procedures in the field of pathology, which is a medical specialty.

Periodic acid is an oxidizing agent with the chemical formula HIO4 or H5IO6. It is often used in histology (the study of the microscopic structure of tissues) to perform a special staining technique called the periodic acid-Schiff (PAS) reaction. This reaction is used to identify certain types of carbohydrates, such as glycogen and some types of mucins, in tissues.

The periodic acid first oxidizes the carbohydrate molecules, creating aldehydes. These aldehydes then react with a Schiff reagent, which results in a pink or magenta color. This reaction can help pathologists identify and diagnose various medical conditions, such as cancer, infection, and inflammation.

Thin-layer chromatography (TLC) is a type of chromatography used to separate, identify, and quantify the components of a mixture. In TLC, the sample is applied as a small spot onto a thin layer of adsorbent material, such as silica gel or alumina, which is coated on a flat, rigid support like a glass plate. The plate is then placed in a developing chamber containing a mobile phase, typically a mixture of solvents.

As the mobile phase moves up the plate by capillary action, it interacts with the stationary phase and the components of the sample. Different components of the mixture travel at different rates due to their varying interactions with the stationary and mobile phases, resulting in distinct spots on the plate. The distance each component travels can be measured and compared to known standards to identify and quantify the components of the mixture.

TLC is a simple, rapid, and cost-effective technique that is widely used in various fields, including forensics, pharmaceuticals, and research laboratories. It allows for the separation and analysis of complex mixtures with high resolution and sensitivity, making it an essential tool in many analytical applications.

Bacterial polysaccharides are complex carbohydrates that consist of long chains of sugar molecules (monosaccharides) linked together by glycosidic bonds. They are produced and used by bacteria for various purposes such as:

1. Structural components: Bacterial polysaccharides, such as peptidoglycan and lipopolysaccharide (LPS), play a crucial role in maintaining the structural integrity of bacterial cells. Peptidoglycan is a major component of the bacterial cell wall, while LPS forms the outer layer of the outer membrane in gram-negative bacteria.
2. Nutrient storage: Some bacteria synthesize and store polysaccharides as an energy reserve, similar to how plants store starch. These polysaccharides can be broken down and utilized by the bacterium when needed.
3. Virulence factors: Bacterial polysaccharides can also function as virulence factors, contributing to the pathogenesis of bacterial infections. For example, certain bacteria produce capsular polysaccharides (CPS) that surround and protect the bacterial cells from host immune defenses, allowing them to evade phagocytosis and persist within the host.
4. Adhesins: Some polysaccharides act as adhesins, facilitating the attachment of bacteria to surfaces or host cells. This is important for biofilm formation, which helps bacteria resist environmental stresses and antibiotic treatments.
5. Antigenic properties: Bacterial polysaccharides can be highly antigenic, eliciting an immune response in the host. The antigenicity of these molecules can vary between different bacterial species or even strains within a species, making them useful as targets for vaccines and diagnostic tests.

In summary, bacterial polysaccharides are complex carbohydrates that serve various functions in bacteria, including structural support, nutrient storage, virulence factor production, adhesion, and antigenicity.

Melibiose is a disaccharide composed of two molecules of galactose. It's formed by the hydrolysis of raffinose, another sugar found in some plants. Melibiose is not as common in nature as other disaccharides like sucrose or lactose, but it can be found in small amounts in certain foods such as honey and some legumes.

Melibiose is not easily digestible by humans because the enzyme that breaks down this sugar, melibiase (also known as alpha-galactosidase), is not produced in significant quantities in the human body. As a result, consuming large amounts of melibiose can lead to gastrointestinal discomfort and symptoms such as bloating, diarrhea, and flatulence.

In summary, melibiose is a relatively uncommon disaccharide composed of two galactose molecules that requires the enzyme melibiase for digestion, which humans do not produce in significant quantities.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

N-Acetylneuraminic Acid (Neu5Ac) is an organic compound that belongs to the family of sialic acids. It is a common terminal sugar found on many glycoproteins and glycolipids on the surface of animal cells. Neu5Ac plays crucial roles in various biological processes, including cell recognition, signaling, and intercellular interactions. It is also involved in the protection against pathogens by serving as a barrier to prevent their attachment to host cells. Additionally, Neu5Ac has been implicated in several disease conditions, such as cancer and inflammation, due to its altered expression and metabolism.

Uronic acids are a type of organic compound that are carboxylic acids derived from sugars (carbohydrates). They are formed by the oxidation of the primary alcohol group (-CH2OH) on a pentose sugar, resulting in a carboxyl group (-COOH) at that position.

The most common uronic acid is glucuronic acid, which is derived from glucose. Other examples include galacturonic acid (derived from galactose), iduronic acid (derived from glucose or galactose), and mannuronic acid (derived from mannose).

Uronic acids play important roles in various biological processes, such as the formation of complex carbohydrates like glycosaminoglycans, which are major components of connective tissues. They also serve as important intermediates in the metabolism of sugars and other carbohydrates.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

Ricin is defined as a highly toxic protein that is derived from the seeds of the castor oil plant (Ricinus communis). It can be produced as a white, powdery substance or a mistable aerosol. Ricin works by getting inside cells and preventing them from making the proteins they need. Without protein, cells die. Eventually, this can cause organ failure and death.

It is not easily inhaled or absorbed through the skin, but if ingested or injected, it can be lethal in very small amounts. There is no antidote for ricin poisoning - treatment consists of supportive care. Ricin has been used as a bioterrorism agent in the past and continues to be a concern due to its relative ease of production and potential high toxicity.

Alpha-galactosidase is an enzyme that breaks down complex carbohydrates, specifically those containing alpha-galactose molecules. This enzyme is found in humans, animals, and microorganisms. In humans, a deficiency of this enzyme can lead to a genetic disorder known as Fabry disease, which is characterized by the accumulation of these complex carbohydrates in various tissues and organs, leading to progressive damage. Alpha-galactosidase is also used as a medication for the treatment of Fabry disease, where it is administered intravenously to help break down the accumulated carbohydrates and alleviate symptoms.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Xylose is a type of sugar that is commonly found in plants and wood. In the context of medical definitions, xylose is often used in tests to assess the function of the small intestine. The most common test is called the "xylose absorption test," which measures the ability of the small intestine to absorb this sugar.

In this test, a patient is given a small amount of xylose to drink, and then several blood and/or urine samples are collected over the next few hours. The amount of xylose that appears in these samples is measured and used to determine how well the small intestine is absorbing nutrients.

Abnormal results on a xylose absorption test can indicate various gastrointestinal disorders, such as malabsorption syndromes, celiac disease, or bacterial overgrowth in the small intestine.

Actinomycetales is an order of Gram-positive bacteria that are characterized by their filamentous morphology and branching appearance, resembling fungi. These bacteria are often found in soil and water, and some species can cause diseases in humans and animals. The name "Actinomycetales" comes from the Greek words "actis," meaning ray or beam, and "mykes," meaning fungus.

The order Actinomycetales includes several families of medical importance, such as Mycobacteriaceae (which contains the tuberculosis-causing Mycobacterium tuberculosis), Corynebacteriaceae (which contains the diphtheria-causing Corynebacterium diphtheriae), and Actinomycetaceae (which contains the actinomycosis-causing Actinomyces israelii).

Actinomycetales are known for their complex cell walls, which contain a unique type of lipid called mycolic acid. This feature makes them resistant to many antibiotics and contributes to their ability to cause chronic infections. They can also form resistant structures called spores, which allow them to survive in harsh environments and contribute to their ability to cause disease.

Overall, Actinomycetales are important both as beneficial soil organisms and as potential pathogens that can cause serious diseases in humans and animals.

Fructose is a simple monosaccharide, also known as "fruit sugar." It is a naturally occurring carbohydrate that is found in fruits, vegetables, and honey. Fructose has the chemical formula C6H12O6 and is a hexose, or six-carbon sugar.

Fructose is absorbed directly into the bloodstream during digestion and is metabolized primarily in the liver. It is sweeter than other sugars such as glucose and sucrose (table sugar), which makes it a popular sweetener in many processed foods and beverages. However, consuming large amounts of fructose can have negative health effects, including increasing the risk of obesity, diabetes, and heart disease.

Neuraminidase is an enzyme that occurs on the surface of influenza viruses. It plays a crucial role in the life cycle of the virus by helping it to infect host cells and to spread from cell to cell within the body. Neuraminidase works by cleaving sialic acid residues from glycoproteins, allowing the virus to detach from infected cells and to move through mucus and other bodily fluids. This enzyme is a major target of antiviral drugs used to treat influenza, such as oseltamivir (Tamiflu) and zanamivir (Relenza). Inhibiting the activity of neuraminidase can help to prevent the spread of the virus within the body and reduce the severity of symptoms.

Beta-galactosidase is an enzyme that catalyzes the hydrolysis of beta-galactosides into monosaccharides. It is found in various organisms, including bacteria, yeast, and mammals. In humans, it plays a role in the breakdown and absorption of certain complex carbohydrates, such as lactose, in the small intestine. Deficiency of this enzyme in humans can lead to a disorder called lactose intolerance. In scientific research, beta-galactosidase is often used as a marker for gene expression and protein localization studies.

Fermentation is a metabolic process in which an organism converts carbohydrates into alcohol or organic acids using enzymes. In the absence of oxygen, certain bacteria, yeasts, and fungi convert sugars into carbon dioxide, hydrogen, and various end products, such as alcohol, lactic acid, or acetic acid. This process is commonly used in food production, such as in making bread, wine, and beer, as well as in industrial applications for the production of biofuels and chemicals.

Hexose phosphates are organic compounds that consist of a hexose sugar molecule (a monosaccharide containing six carbon atoms, such as glucose or fructose) that has been phosphorylated, meaning that a phosphate group has been added to it. This process is typically facilitated by enzymes called kinases, which transfer a phosphate group from a donor molecule (usually ATP) to the sugar molecule.

Hexose phosphates play important roles in various metabolic pathways, including glycolysis, gluconeogenesis, and the pentose phosphate pathway. For example, glucose-6-phosphate is a key intermediate in both glycolysis and gluconeogenesis, while fructose-6-phosphate and fructose-1,6-bisphosphate are important intermediates in glycolysis. The pentose phosphate pathway, which is involved in the production of NADPH and ribose-5-phosphate, begins with the conversion of glucose-6-phosphate to 6-phosphogluconolactone by the enzyme glucose-6-phosphate dehydrogenase.

Overall, hexose phosphates are important metabolic intermediates that help regulate energy production and utilization in cells.

A cell wall is a rigid layer found surrounding the plasma membrane of plant cells, fungi, and many types of bacteria. It provides structural support and protection to the cell, maintains cell shape, and acts as a barrier against external factors such as chemicals and mechanical stress. The composition of the cell wall varies among different species; for example, in plants, it is primarily made up of cellulose, hemicellulose, and pectin, while in bacteria, it is composed of peptidoglycan.

Uridine Diphosphate Glucose (UDP-glucose) is a nucleotide sugar that plays a crucial role in the synthesis and metabolism of carbohydrates in the body. It is formed from uridine triphosphate (UTP) and glucose-1-phosphate through the action of the enzyme UDP-glucose pyrophosphorylase.

UDP-glucose serves as a key intermediate in various biochemical pathways, including glycogen synthesis, where it donates glucose molecules to form glycogen, a large polymeric storage form of glucose found primarily in the liver and muscles. It is also involved in the biosynthesis of other carbohydrate-containing compounds such as proteoglycans and glycolipids.

Moreover, UDP-glucose is an essential substrate for the enzyme glucosyltransferase, which is responsible for adding glucose molecules to various acceptor molecules during the process of glycosylation. This post-translational modification is critical for the proper folding and functioning of many proteins.

Overall, UDP-glucose is a vital metabolic intermediate that plays a central role in carbohydrate metabolism and protein function.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

UTP-Glucose-1-Phosphate Uridylyltransferase is an enzyme that catalyzes the reaction to form UDP-glucose from UTP and glucose-1-phosphate. This reaction plays a crucial role in the biosynthesis of various carbohydrates, glycoproteins, and glycolipids in the body. The enzyme is also known as UDP-glucose pyrophosphorylase or simply as UGPase.

The systematic name for this enzyme is glucose-1-phosphate:UTP uridylyltransferase, and its reaction can be represented as follows:
UTP + glucose-1-phosphate ⇌ UDP-glucose + pyrophosphate

The enzyme is widely distributed in nature and is found in various organisms, including bacteria, plants, and animals. In humans, UGPase is present in multiple tissues, such as the liver, kidney, and brain. Defects in this enzyme can lead to several metabolic disorders, highlighting its importance in maintaining normal bodily functions.

Monosaccharide transport proteins are a type of membrane transport protein that facilitate the passive or active transport of monosaccharides, such as glucose, fructose, and galactose, across cell membranes. These proteins play a crucial role in the absorption, distribution, and metabolism of carbohydrates in the body.

There are two main types of monosaccharide transport proteins: facilitated diffusion transporters and active transporters. Facilitated diffusion transporters, also known as glucose transporters (GLUTs), passively transport monosaccharides down their concentration gradient without the need for energy. In contrast, active transporters, such as the sodium-glucose cotransporter (SGLT), use energy in the form of ATP to actively transport monosaccharides against their concentration gradient.

Monosaccharide transport proteins are found in various tissues throughout the body, including the intestines, kidneys, liver, and brain. They play a critical role in maintaining glucose homeostasis by regulating the uptake and release of glucose into and out of cells. Dysfunction of these transporters has been implicated in several diseases, such as diabetes, cancer, and neurological disorders.

"Lactococcus lactis" is a species of gram-positive, facultatively anaerobic bacteria that are commonly found in nature, particularly in environments involving plants and dairy products. It is a catalase-negative, non-spore forming coccus that typically occurs in pairs or short chains.

"Lactococcus lactis" has significant industrial importance as it plays a crucial role in the production of fermented foods such as cheese and buttermilk. The bacterium converts lactose into lactic acid, which contributes to the sour taste and preservative qualities of these products.

In addition to its use in food production, "Lactococcus lactis" has been explored for its potential therapeutic applications. It can be used as a vector for delivering therapeutic proteins or vaccines to the gastrointestinal tract due to its ability to survive and colonize there.

It's worth noting that "Lactococcus lactis" is generally considered safe for human consumption, and it's one of the most commonly used probiotics in food and supplements.

Ribose is a simple carbohydrate, specifically a monosaccharide, which means it is a single sugar unit. It is a type of sugar known as a pentose, containing five carbon atoms. Ribose is a vital component of ribonucleic acid (RNA), one of the essential molecules in all living cells, involved in the process of transcribing and translating genetic information from DNA to proteins. The term "ribose" can also refer to any sugar alcohol derived from it, such as D-ribose or Ribitol.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Phlorhizin is not a medical condition or term, but rather a chemical compound. It is a glucoside that can be found in the bark of apple trees and other related plants. Phlorhizin has been studied in the field of medicine for its potential effects on various health conditions. Specifically, it has been shown to inhibit the enzyme called glucose transporter 2 (GLUT2), which is involved in the absorption of glucose in the body. As a result, phlorhizin has been investigated as a potential treatment for diabetes, as it may help regulate blood sugar levels. However, more research is needed to fully understand its effects and safety profile before it can be used as a medical treatment.

Globosides are a type of glycosphingolipids, which are molecules that consist of a lipid and a carbohydrate. They are found in animal tissues, especially in the nervous system. The term "globoside" refers to a specific structure of these molecules, where the carbohydrate portion consists of a complex chain of sugars, including galactose, N-acetylgalactosamine, and glucose. Globosides play important roles in cell recognition and interaction, and abnormalities in their metabolism have been associated with certain diseases, such as paroxysmal nocturnal hemoglobinuria (PNH).

Chromatography, gas (GC) is a type of chromatographic technique used to separate, identify, and analyze volatile compounds or vapors. In this method, the sample mixture is vaporized and carried through a column packed with a stationary phase by an inert gas (carrier gas). The components of the mixture get separated based on their partitioning between the mobile and stationary phases due to differences in their adsorption/desorption rates or solubility.

The separated components elute at different times, depending on their interaction with the stationary phase, which can be detected and quantified by various detection systems like flame ionization detector (FID), thermal conductivity detector (TCD), electron capture detector (ECD), or mass spectrometer (MS). Gas chromatography is widely used in fields such as chemistry, biochemistry, environmental science, forensics, and food analysis.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

An asialoglycoprotein receptor (ASGPR) is a type of cell surface receptor found primarily on hepatocytes, which are the main cell type in the liver. These receptors are responsible for recognizing and removing glycoproteins (proteins with attached carbohydrate molecules) from circulation, particularly those that have lost their terminal sialic acid residues through a process called desialylation.

ASGPRs play an essential role in the liver's clearance function by identifying and removing various substances, such as bacteria, viruses, and abnormal or damaged cells, from the bloodstream. There are two main types of ASGPRs, known as ASGPR1 and ASGPR2, which have different structures and functions but work together to mediate the endocytosis and degradation of desialylated glycoproteins.

Understanding the role of ASGPRs in liver function has important implications for developing targeted therapies and diagnostic tools for various liver-related diseases, including hepatitis, cirrhosis, and liver cancer.

Sodium-glucose transport proteins (SGLTs) are a group of membrane transporters that facilitate the active transport of glucose across cell membranes in various tissues, including the kidneys and intestines. They function by coupling the movement of glucose molecules with sodium ions, using the energy generated by the sodium gradient across the membrane.

The two main types of SGLTs are:

1. SGLT1: This transporter is primarily found in the intestines and plays a crucial role in glucose absorption from food. It has a high affinity for glucose and transports it along with sodium ions, which helps create an electrochemical gradient that drives the transport process.

2. SGLT2: This transporter is mainly located in the early proximal tubules of the kidneys and is responsible for reabsorbing about 90% of the filtered glucose back into the bloodstream. It has a lower affinity for glucose compared to SGLT1 but operates at a higher transport rate, allowing it to efficiently reabsorb large amounts of glucose.

Inhibitors of SGLT2, known as SGLT2 inhibitors or gliflozins, have been developed for the treatment of type 2 diabetes. By blocking SGLT2-mediated glucose reabsorption in the kidneys, these medications promote urinary glucose excretion and help lower blood glucose levels. Examples of SGLT2 inhibitors include canagliflozin, dapagliflozin, and empagliflozin.

Galactans are a type of complex carbohydrates known as oligosaccharides that are composed of galactose molecules. They can be found in certain plants, including beans, lentils, and some fruits and vegetables. In the human body, galactans are not digestible and can reach the colon intact, where they may serve as a substrate for fermentation by gut bacteria. This can lead to the production of short-chain fatty acids, which have been shown to have various health benefits. However, in some individuals with irritable bowel syndrome or other functional gastrointestinal disorders, consumption of galactans may cause digestive symptoms such as bloating, gas, and diarrhea.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

'Erythrina' is a botanical term, not a medical one. It refers to a genus of plants in the family Fabaceae, also known as the pea or legume family. These plants are commonly called coral trees due to their bright red flowers. While some parts of certain species can have medicinal uses, such as anti-inflammatory and analgesic properties, 'Erythrina' itself is not a medical term or condition.

Culture media is a substance that is used to support the growth of microorganisms or cells in an artificial environment, such as a petri dish or test tube. It typically contains nutrients and other factors that are necessary for the growth and survival of the organisms being cultured. There are many different types of culture media, each with its own specific formulation and intended use. Some common examples include blood agar, which is used to culture bacteria; Sabouraud dextrose agar, which is used to culture fungi; and Eagle's minimum essential medium, which is used to culture animal cells.

Kluyveromyces is a genus of ascomycetous yeasts, which are commonly found in various environments such as plant material, food, and dairy products. These yeasts are often used in industrial applications, including the production of biofuels, enzymes, and single-cell proteins. Some species of Kluyveromyces have probiotic properties and can be found in the gastrointestinal tracts of animals and humans.

The genus Kluyveromyces is named after the Dutch microbiologist Albert J. Kluyver, who made significant contributions to the field of yeast research. The taxonomy of this genus has undergone several revisions, and some species previously classified as Kluyveromyces have been reassigned to other genera.

It is important to note that while Kluyveromyces species are generally considered safe for industrial use and human consumption, they can still cause infections in immunocompromised individuals or those with underlying medical conditions. Therefore, it is essential to handle these organisms with care and follow appropriate safety protocols when working with them.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Glycoconjugates are a type of complex molecule that form when a carbohydrate (sugar) becomes chemically linked to a protein or lipid (fat) molecule. This linkage, known as a glycosidic bond, results in the formation of a new molecule that combines the properties and functions of both the carbohydrate and the protein or lipid component.

Glycoconjugates can be classified into several categories based on the type of linkage and the nature of the components involved. For example, glycoproteins are glycoconjugates that consist of a protein backbone with one or more carbohydrate chains attached to it. Similarly, glycolipids are molecules that contain a lipid anchor linked to one or more carbohydrate residues.

Glycoconjugates play important roles in various biological processes, including cell recognition, signaling, and communication. They are also involved in the immune response, inflammation, and the development of certain diseases such as cancer and infectious disorders. As a result, understanding the structure and function of glycoconjugates is an active area of research in biochemistry, cell biology, and medical science.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Methylglycosides are not a recognized medical term or concept. However, in chemistry, methylglycosides refer to glycosidic compounds in which the glycosidic linkage is formed between a hemiacetal or hemiketal of a monosaccharide and a methanol molecule. These compounds are not typically associated with medical definitions or applications, but rather fall under the broader categories of organic chemistry or biochemistry.

Cerebrosides are a type of sphingolipid, which are lipids that contain sphingosine. They are major components of the outer layer of cell membranes and are particularly abundant in the nervous system. Cerebrosides are composed of a ceramide molecule (a fatty acid attached to sphingosine) and a sugar molecule, usually either glucose or galactose.

Glycosphingolipids that contain a ceramide with a single sugar residue are called cerebrosides. Those that contain more complex oligosaccharide chains are called gangliosides. Cerebrosides play important roles in cell recognition, signal transduction, and cell adhesion.

Abnormalities in the metabolism of cerebrosides can lead to various genetic disorders, such as Gaucher's disease, Krabbe disease, and Fabry disease. These conditions are characterized by the accumulation of cerebrosides or their breakdown products in various tissues, leading to progressive damage and dysfunction.

Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.

Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.

Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.

Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Gene expression regulation in fungi refers to the complex cellular processes that control the production of proteins and other functional gene products in response to various internal and external stimuli. This regulation is crucial for normal growth, development, and adaptation of fungal cells to changing environmental conditions.

In fungi, gene expression is regulated at multiple levels, including transcriptional, post-transcriptional, translational, and post-translational modifications. Key regulatory mechanisms include:

1. Transcription factors (TFs): These proteins bind to specific DNA sequences in the promoter regions of target genes and either activate or repress their transcription. Fungi have a diverse array of TFs that respond to various signals, such as nutrient availability, stress, developmental cues, and quorum sensing.
2. Chromatin remodeling: The organization and compaction of DNA into chromatin can influence gene expression. Fungi utilize ATP-dependent chromatin remodeling complexes and histone modifying enzymes to alter chromatin structure, thereby facilitating or inhibiting the access of transcriptional machinery to genes.
3. Non-coding RNAs: Small non-coding RNAs (sncRNAs) play a role in post-transcriptional regulation of gene expression in fungi. These sncRNAs can guide RNA-induced transcriptional silencing (RITS) complexes to specific target loci, leading to the repression of gene expression through histone modifications and DNA methylation.
4. Alternative splicing: Fungi employ alternative splicing mechanisms to generate multiple mRNA isoforms from a single gene, thereby increasing proteome diversity. This process can be regulated by RNA-binding proteins that recognize specific sequence motifs in pre-mRNAs and promote or inhibit splicing events.
5. Protein stability and activity: Post-translational modifications (PTMs) of proteins, such as phosphorylation, ubiquitination, and sumoylation, can influence their stability, localization, and activity. These PTMs play a crucial role in regulating various cellular processes, including signal transduction, stress response, and cell cycle progression.

Understanding the complex interplay between these regulatory mechanisms is essential for elucidating the molecular basis of fungal development, pathogenesis, and drug resistance. This knowledge can be harnessed to develop novel strategies for combating fungal infections and improving agricultural productivity.

Gangliosides are a type of complex lipid molecule known as sialic acid-containing glycosphingolipids. They are predominantly found in the outer leaflet of the cell membrane, particularly in the nervous system. Gangliosides play crucial roles in various biological processes, including cell recognition, signal transduction, and cell adhesion. They are especially abundant in the ganglia (nerve cell clusters) of the peripheral and central nervous systems, hence their name.

Gangliosides consist of a hydrophobic ceramide portion and a hydrophilic oligosaccharide chain that contains one or more sialic acid residues. The composition and structure of these oligosaccharide chains can vary significantly among different gangliosides, leading to the classification of various subtypes, such as GM1, GD1a, GD1b, GT1b, and GQ1b.

Abnormalities in ganglioside metabolism or expression have been implicated in several neurological disorders, including Parkinson's disease, Alzheimer's disease, and various lysosomal storage diseases like Tay-Sachs and Gaucher's diseases. Additionally, certain bacterial toxins, such as botulinum neurotoxin and tetanus toxin, target gangliosides to gain entry into neuronal cells, causing their toxic effects.

A trisaccharide is a type of carbohydrate molecule composed of three monosaccharide units joined together by glycosidic bonds. Monosaccharides are simple sugars, such as glucose, fructose, and galactose, which serve as the building blocks of more complex carbohydrates.

In a trisaccharide, two monosaccharides are linked through a glycosidic bond to form a disaccharide, and then another monosaccharide is attached to the disaccharide via another glycosidic bond. The formation of these bonds involves the loss of a water molecule (dehydration synthesis) between the hemiacetal or hemiketal group of one monosaccharide and the hydroxyl group of another.

Examples of trisaccharides include raffinose (glucose + fructose + galactose), maltotriose (glucose + glucose + glucose), and melezitose (glucose + fructose + glucose). Trisaccharides can be found naturally in various foods, such as honey, sugar beets, and some fruits and vegetables. They play a role in energy metabolism, serving as an energy source for the body upon digestion into monosaccharides, which are then absorbed into the bloodstream and transported to cells for energy production or storage.

N-Acetyllactosamine Synthase (Galβ1,3GlcNAc-T) is an enzyme that catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to a terminal β-D-galactose residue of glycoproteins or glycolipids, forming β1,3 linkages and creating the disaccharide N-acetyllactosamine (Galβ1-3GlcNAc). This enzyme plays a crucial role in the biosynthesis of complex carbohydrates called mucin-type O-glycans and some types of A, B, H, Le^a^, and Le^b^ blood group antigens. There are two major isoforms of this enzyme, β3GnT1 and β3GnT2, which differ in their substrate specificities and tissue distributions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Sialyltransferases are a group of enzymes that play a crucial role in the biosynthesis of sialic acids, which are a type of sugar molecule found on the surface of many cell types. These enzymes catalyze the transfer of sialic acid from a donor molecule (usually CMP-sialic acid) to an acceptor molecule, such as a glycoprotein or glycolipid.

The addition of sialic acids to these molecules can affect their function and properties, including their recognition by other cells and their susceptibility to degradation. Sialyltransferases are involved in various biological processes, including cell-cell recognition, inflammation, and cancer metastasis.

There are several different types of sialyltransferases, each with specific substrate preferences and functions. For example, some sialyltransferases add sialic acids to the ends of N-linked glycans, while others add them to O-linked glycans or glycolipids.

Abnormalities in sialyltransferase activity have been implicated in various diseases, including cancer, inflammatory disorders, and neurological conditions. Therefore, understanding the function and regulation of these enzymes is an important area of research with potential implications for disease diagnosis and treatment.

An operon is a genetic unit in prokaryotic organisms (like bacteria) consisting of a cluster of genes that are transcribed together as a single mRNA molecule, which then undergoes translation to produce multiple proteins. This genetic organization allows for the coordinated regulation of genes that are involved in the same metabolic pathway or functional process. The unit typically includes promoter and operator regions that control the transcription of the operon, as well as structural genes encoding the proteins. Operons were first discovered in bacteria, but similar genetic organizations have been found in some eukaryotic organisms, such as yeast.

A disaccharide composed of two units of galactose, galactose-alpha-1,3-galactose (alpha-gal), has been recognized as a ... phosphorylates α-D-galactose to galactose-1-phosphate, or Gal-1-P; Galactose-1-phosphate uridyltransferase (GALT) transfers a ... A galactose molecule linked with a glucose molecule forms a lactose molecule. Galactan is a polymeric form of galactose found ... Galactose metabolism, which converts galactose into glucose, is carried out by the three principal enzymes in a mechanism known ...
... (aldose 1-epimerase) (gene name GALM) is a human enzyme that converts alpha-aldose to the beta-anomer. ... This enzyme catalyzes the first step of the Leloir Pathway, which is involved in galactose metabolism. It belongs to family of ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Aldose 1-epimerase (Galactose ... Thoden, James B.; Timson, David J.; Reece, Richard J.; Holden, Hazel M. (2004-05-01). "Molecular Structure of Human Galactose ...
Galactose is the self-released debut EP by The Dead Science under their original name 'The Sweet Science'. "The Satin Glove" - ... 5:35 "Prefect" - 4:21 "Galactose" - 3:47 "Curtain" - 2:31 "I Don't Believe" - 6:17 "Endless Cities" - 4:32 "Tangle Eye" - 3:31 ...
... (D-galactose:oxygen 6-oxidoreductase, D-galactose oxidase, beta-galactose oxidase; abbreviated GAO, GAOX, ... Galactose oxidase belongs to the family of oxidoreductases. Copper ion is required as a cofactor for galactose oxidase. A ... In fact, galactose oxidase catalyzes dihydroxyacetone three times faster than it does to galactose. The reaction is ... In yeasts, galactose oxidase catalyzes the following reaction: D-galactose + O2 ⇌ {\displaystyle \rightleftharpoons } D-galacto ...
Galactose UDP galactose epimerase Uridine diphosphate "Galactose 1 Phosphate Uridyltransferase Deficiency". StatPearls. ... Uridine diphosphate galactose (UDP-galactose) is an intermediate in the production of polysaccharides. It is important in ...
... , also known as GALE deficiency, Galactosemia III and UDP-galactose-4-epimerase deficiency, is a ... UDP-Galactose-4-Epimerase - 606953 Lai K, Elsas LJ, Wierenga KJ (November 2009). "Galactose toxicity in animals". IUBMB Life. ... preventing the formation of glucose-1-phosphate and leading to the accumulation of galactose and galactose-1-phosphate. High ... Park HD, Park KU, Kim JQ, Shin CH, Yang SW, Lee DH, Song YH, Song J (November 2005). "The molecular basis of UDP-galactose-4- ...
"Association of the Golgi UDP-galactose transporter with UDP-galactose:ceramide galactosyltransferase allows UDP-galactose ... UDP-galactose translocator is a protein that in humans is encoded by the SLC35A2 gene. Variants of the SLC35A2 gene haven ... Yoshioka S, Sun-Wada GH, Ishida N, Kawakita M (October 1997). "Expression of the human UDP-galactose transporter in the Golgi ... Hara T, Yamauchi M, Takahashi E, Hoshino M, Aoki K, Ayusawa D, Kawakita M (November 1993). "The UDP-galactose translocator gene ...
Rees DA (November 1961). "Enzymic synthesis of 3:6-anhydro-l-galactose within porphyran from l-galactose 6-sulphate units". The ... galactose-6-sulfatase, and galactose 6-sulfatase. Rees DA (September 1961). "Enzymic desulphation of porphyran". The ... In enzymology, a galactose-6-sulfurylase (EC 2.5.1.5) is an enzyme that catalyzes the chemical reaction Eliminates sulfate from ... The systematic name of this enzyme class is D-galactose-6-sulfate:alkyltransferase (cyclizing). Other names in common use ...
In enzymology, a dTDP-galactose 6-dehydrogenase (EC 1.1.1.186) is an enzyme that catalyzes the chemical reaction dTDP-D- ... The systematic name of this enzyme class is dTDP-D-galactose:NADP+ 6-oxidoreductase. This enzyme is also called thymidine- ... 2 H+ The 3 substrates of this enzyme are dTDP-D-galactose, NADP+, and H2O, whereas its 3 products are dTDP-D-galacturonate, ... diphosphate-galactose dehydrogenase. This enzyme participates in nucleotide sugars metabolism. Katan R, Avigad G (1966). "NADP ...
In enzymology, a galactose 1-dehydrogenase (NADP+) (EC 1.1.1.120) is an enzyme that catalyzes the chemical reaction D-galactose ... The systematic name of this enzyme class is D-galactose:NADP+ 1-oxidoreductase. Other names in common use include D-galactose ... dehydrogenase (NADP+), and galactose 1-dehydrogenase (NADP+). This enzyme participates in galactose metabolism. Cline AL, Hu AS ... the two substrates of this enzyme are D-galactose and NADP+, whereas its 3 products are D-galactonolactone, NADPH, and H+. This ...
galactose glucose GALT catalyzes the second reaction of the Leloir pathway of galactose metabolism through ping pong bi-bi ... Galactose-1-phosphate uridyltransferase (GALT) catalyzes the second step of the Leloir pathway of galactose metabolism, namely ... UDP-glucose + E-His ⇌ Glucose-1-phosphate + E-His-UMP Galactose-1-phosphate + E-His-UMP ⇌ UDP-galactose + E-His The three- ... "Entrez Gene: GALT galactose-1-phosphate uridylyltransferase". Wong LJ, Frey PA (September 1974). "Galactose-1-phosphate ...
... (EC 2.7.7.69, VTC2, VTC5) is an enzyme with systematic name GDP:alpha-L-galactose 1-phosphate ... GDP-L-galactose+phosphorylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.7. ... Linster CL, Adler LN, Webb K, Christensen KC, Brenner C, Clarke SG (July 2008). "A second GDP-L-galactose phosphorylase in ... This enzyme catalyses the following chemical reaction GDP-L-galactose + phosphate ⇌ {\displaystyle \rightleftharpoons } alpha-L ...
The systematic name of this enzyme class is UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase. Other names in ... In enzymology, an undecaprenyl-phosphate galactose phosphotransferase (EC 2.7.8.6) is an enzyme that catalyzes the chemical ... the two substrates of this enzyme are UDP-galactose and undecaprenyl phosphate, whereas its two products are UMP and alpha-D- ... reaction UDP-galactose + undecaprenyl phosphate ⇌ {\displaystyle \rightleftharpoons } UMP + alpha-D-galactosyl- ...
Other names in common use include dTDP galactose pyrophosphorylase, galactose 1-phosphate thymidylyl transferase, thymidine ... dTDP-galactose Thus, the two substrates of this enzyme are dTTP and alpha-D-galactose 1-phosphate, whereas its two products are ... alpha-D-galactose 1-phosphate thymidylyltransferase from Streptococcus faecalis grown on D-galactose". The Journal of ... In enzymology, a galactose-1-phosphate thymidylyltransferase (EC 2.7.7.32) is an enzyme that catalyzes the chemical reaction ...
... s is a family of several mammalian galactose-3-O-sulfotransferase proteins. Gal-3-O- ...
L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure. A cysteine- ... In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the ... rich domain (the galactose binding lectin domain) homologous to the SUEL protein has been identified in the following proteins ... The galactose-binding lectin domain is not required for alpha-latratoxin binding. Human latrophilin-1. Human Latrophilin-2. ...
... (EC 1.1.1.316, L-GalDH, L-galactose dehydrogenase) is an enzyme with the systematic name L- ... galactose:NAD+ 1-oxidoreductase. This enzyme catalyses the following chemical reaction: L-galactose + NAD+ ⇌ {\displaystyle \ ... L-galactose+1-dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.1.1) ... Gatzek S, Wheeler GL, Smirnoff N (June 2002). "Antisense suppression of l-galactose dehydrogenase in Arabidopsis thaliana ...
... glucose and galactose. In the first step of galactose metabolism, galactose is converted to galactose-1-phosphate (Gal-1-P) by ... Gal-1-P is converted to uridine diphosphate galactose (UDP-galactose) by the enzyme galactose-1-phosphate uridylyltransferase, ... "Distinct roles of galactose-1P in galactose-mediated growth arrest of yeast deficient in galactose-1P uridylyltransferase (GALT ... UDP-galactose can then be converted to lactose, by the enzyme lactose synthase or to UDP-glucose by UDP-galactose epimerase ( ...
Galactose-α-1,3-galactose, commonly known as alpha gal and the Galili antigen, is a carbohydrate found in most mammalian cell ... "Identification of galactose-α-1,3-galactose in the gastrointestinal tract of the tick Ixodes ricinus; possible relationship ... Alpha-gal allergy Galactose Singh, S., Thompson, J. A., Yilmaz, B., Li, H., Weis, S., Sobral, D., Truglio, M., Aires da Silva, ...
The systematic name of this enzyme class is UDP-galactose:UDP-N-acetyl-D-glucosamine galactose phosphotransferase. Other names ... In enzymology, an UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase (EC 2.7.8.18) is an enzyme that catalyzes ... D-galactose-1-phospho)-D-glucosamine Thus, the two substrates of this enzyme are UDP-galactose and UDP-N-acetyl-D-glucosamine, ... Nakanishi Y, Otsu K, Suzuki S (1983). "Enzymatic transfer of galactosyl phosphate from UDP-galactose to UDP-N-acetylglucosamine ...
The galactose component originates from UDP-galactose and the GalNAc component originates from UDP-N-acetylgalactosamine. These ... Overlapping and distinct roles of Aspergillus fumigatus UDP-glucose 4-epimerases in galactose metabolism and the synthesis of ... Galactosaminogalactan (commonly abbreviated as GAG or GG), is an exopolysaccharide composed of galactose and N- ... galactose-containing cell wall polysaccharides. J Biol Chem. 2014 Jan 17;289(3):1243-56. (Polysaccharides, Galactose). ...
Typically, the severe diarrhea improves with a diet low in glucose/galactose and the tolerability to glucose/galactose improves ... Glucose-galactose malabsorption, a genetic disorder caused by changes in a protein critical for the transport of glucose and ... "Glucose-galactose malabsorption , Genetic and Rare Diseases Information Center (GARD) - an NCATS Program". rarediseases.info. ... galactose across the intestine which leads to impaired glucose/galactose absorption, dehydration, and severe diarrhea in young ...
A Core 1 structure is generated by the addition of galactose. A Core 2 structure is generated by the addition of N-acetyl- ... These are formed by the repetitive addition of galactose and N-acetyl-glucosamine units. Polylactosamine chains on O-linked ... White square = N-acetyl-galactosamine; black circle = galactose; Black square = N-acetyl-glucosamine. Note: There is a mistake ... galactose, neuraminic acid, N-acetylglucosamine, fucose, mannose, and other monosaccharides. In eukaryotes, N-linked glycans ...
MC2R Glucose-galactose malabsorption; 606824; SLC5A1 GLUT1 deficiency syndrome 1; 606777; SLC2A1 GLUT1 deficiency syndrome 2; ... GALK1 Galactose epimerase deficiency; 230350; GALE Galactosemia; 230400; GALT Galactosialidosis; 256540; CTSA Gallbladder ...
Causes the elevation of galactose in blood (galactosemia) and urine (galactosuria). When the patient consumes galactose via ... Diagnosis is established by high blood levels of galactose, normal activity of the enzyme galactose-1-phosphate ... disorder marked by an accumulation of galactose and galactitol secondary to the decreased conversion of galactose to galactose- ... Galactokinase catalyzes the first step of galactose phosphorylation in the Leloir pathway of intermediate metabolism. ...
V: Transformation de la galactose. Les tagatoses, et la galtose" [Action of alkalis on sugars. V: Transformation of galactose. ...
Louis Pasteur crystallizes galactose. Charles-Adolphe Wurtz discovers the glycols. May 20 - Dr David Livingstone arrives at ...
β-Galactosides include carbohydrates containing galactose where the glycosidic bond lies above the galactose molecule. ... β-Galactose is used in such dairy products as yogurt, sour cream, and some cheeses which are treated with the enzyme to break ... When water participates in the reaction, galactose is formed, otherwise, when D-glucose acts as the acceptor in the second step ... It can also hydrolyze lactose into galactose and glucose which will proceed into glycolysis. The active site of β-galactosidase ...
... which is used in the final step of galactose metabolism - catalyzing the reversible conversion of UDP-galactose to UDP-glucose ... Galactose epimerase deficiency Tanner, ME. (2002). "Understanding nature's strategies for enzyme-catalyzed racemization and ...
Abbott WM, Mellor A, Edwards Y, Feizi T (April 1989). "Soluble bovine galactose-binding lectin. cDNA cloning reveals the ...
D-Galactose-1-phosphate is an intermediate in the intraconversion of glucose and uridine diphosphate galactose. It is formed ... The Leloir pathway is responsible for such metabolism of galactose and its intermediate, galactose-1-phosphate. Deficiency of ... Galactose-1-phosphate uridylyltransferase "Galactose 1 Phosphate Uridyltransferase Deficiency (Galactosemia)". StatPearls. ... Utility of Galactose, Galactitol, Galactonate, and Galactose 1-Phosphate". Clinical Chemistry. 56 (7): 1177-1182. doi:10.1373/ ...
"Orphanet: Glucose galactose malabsorption". Glucose galactose malabsorption. National Center for Biotechnology Information (US ... Glucose-galactose malabsorption is a rare condition in which the cells lining the intestine cannot take in the sugars glucose ... Glucose and galactose are called simple sugars, or monosaccharides. Sucrose and lactose are called disaccharides because they ... However, they are able to digest fructose-based formulas that do not contain glucose or galactose. Some affected children are ...
Other names in common use include D-galactose dehydrogenase, beta-galactose dehydrogenase, and NAD+-dependent D-galactose ... In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction D-galactose + NAD+ ... This enzyme participates in galactose metabolism. De Ley J, Doudoroff M (1957). "The metabolism of D-galactose in Pseudomonas ... The systematic name of this enzyme class is D-galactose:NAD+ 1-oxidoreductase. ...
"Methyl-alpha-d-galactose". pubchem.ncbi.nlm.nih.gov. National Library of Medicine. Archived from the original on 2022-08-20. ... Methyl-α-D-galactose is a constituent of Eleutherococcus senticosus. No authors Listed (2021-05-17). Eleuthero. NBK501806 (1st ... Galactose, Monosaccharide derivatives, All stub articles, Organic compound stubs). ...
In enzymology, a galactose-6-phosphate isomerase (EC 5.3.1.26) is an enzyme that catalyzes the chemical reaction D-galactose 6- ... The systematic name of this enzyme class is D-galactose-6-phosphate aldose-ketose-isomerase. This enzyme participates in ... phosphate ⇌ {\displaystyle \rightleftharpoons } D-tagatose 6-phosphate Hence, this enzyme has one substrate, D-galactose 6- ... galactose metabolism. de Vos WM, Boerrigter I, van Rooyen RJ, Reiche B, Hengstenberg W (1990). "Characterization of the lactose ...
6-dideoxy-alpha-D-galactose TDP-4-acetamido-4,6-dideoxy-D-galactose takes part in the biosynthesis of enterobacterial common ... DTDP-4-amino-4,6-dideoxy-D-galactose+acyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... DTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase (EC 2.3.1.210, TDP-fucosamine acetyltransferase, WECD, RFFC) is an enzyme ... This enzyme catalyses the following chemical reaction acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose ⇌ {\displaystyle ...
"Email from Leon, 2012". galactose.neocities.org. Retrieved 2020-05-06. Levee Blues at AllMusic. Retrieved November 14, 2016. ( ...
A disaccharide composed of two units of galactose, galactose-alpha-1,3-galactose (alpha-gal), has been recognized as a ... phosphorylates α-D-galactose to galactose-1-phosphate, or Gal-1-P; Galactose-1-phosphate uridyltransferase (GALT) transfers a ... A galactose molecule linked with a glucose molecule forms a lactose molecule. Galactan is a polymeric form of galactose found ... Galactose metabolism, which converts galactose into glucose, is carried out by the three principal enzymes in a mechanism known ...
... the sugars glucose and galactose, which primarily results in severe diarrhea. Explore symptoms, inheritance, genetics of this ... Glucose-galactose malabsorption is a condition in which the body cannot take in (absorb) ... Glucose-galactose malabsorption is a condition in which the body cannot take in (absorb) the sugars glucose and galactose, ... Glucose and galactose are simple sugars; they are present in many foods, or they can be obtained from the breakdown of lactose ...
α-D-galactose (CHEBI:28061) is a D-galactopyranose (CHEBI:4139) α-D-galactose (CHEBI:28061) is enantiomer of α-L-galactose ( ... penta-O-acetyl-α-D-galactose (CHEBI:63145) has functional parent α-D-galactose (CHEBI:28061). α-L-galactose (CHEBI:42905) is ... D-galactose (CHEBI:28061). 2-deoxy-2-fluoro-α-D-galactose (CHEBI:49143) has functional parent α-D-galactose (CHEBI:28061). N-[( ... α-D-GalpNAc-(1→3)-α-D-Galp (CHEBI:146643) has functional parent α-D-galactose (CHEBI:28061). α-D-galactose 1-phosphate (CHEBI: ...
First described in a variant patient in 1935 by Mason and Turner, galactose-1-phosphate uridyltransferase (GALT) deficiency is ... Uridine diphosphate (UDP) galactose-4-epimerase epimerizes UDP galactose to UDP glucose and is also uncommon. [13] ... Galactose-1-Phosphate Uridyltransferase Deficiency (Galactosemia) * Sections Galactose-1-Phosphate Uridyltransferase Deficiency ... Galactokinase converts galactose to galactose-1-phosphate and is not a common deficiency. ...
Galactose is a space combat/tactical RTS hybrid, which pits hundreds of ships against each other in the age-old war between ... Galactose is a space combat/tactical RTS hybrid, which pits hundreds of ships against each other in the age-old war between ... Will you heed its call? Galactose is a fast-paced space combat which melds fast paced space combat with tactical RTS strategy. ...
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b.18.1: Galactose-binding domain-like [49785] (19 families) More info for Fold b.18: Galactose-binding domain-like. Timeline ... Fold b.18: Galactose-binding domain-like appears in SCOP 1.63. *Fold b.18: Galactose-binding domain-like appears in SCOP 1.67. ... Fold b.18: Galactose-binding domain-like [49784] (1 superfamily). sandwich; 9 strands in 2 sheets; jelly-roll. ... Lineage for Fold b.18: Galactose-binding domain-like. *Root: SCOP 1.65 *. Class b: All beta proteins [48724] (126 folds). ...
A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) exhibited ... Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. ... Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. ... Background: A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) ...
Since the metabolism of galactose is dependent on liver blood flow and hepatic functional mass, further studies are needed. ... test assesses functioning liver mass by measuring the galactose concentration in the blood 1 hour after its administration. The ... i,Aim,/i,. The galactose single-point (GSP) ... and the hepatic clearance of galactose was similar (pre-HD 410 ... The average galactose infusion time was minutes. The predialysis galactose level was g/mL. Six (8%) of the patients were ...
... recovery and follow-up care for Galactose-1-phosphate uridyltransferase blood test. ... Learn about Galactose-1-phosphate uridyltransferase blood test, find a doctor, complications, outcomes, ... Galactose-1-phosphate - blood. In: Chernecky CC, Berger BJ, eds. Laboratory Tests and Diagnostic Procedures. 6th ed. St Louis, ... Galactose-1-phosphate uridyltransferase is a blood test that measures the level of a substance called GALT, which helps break ...
D-Galactose (1-¹³C, 99%) microbiological/pyrogen tested. Item No.CLM-744-MPT-PK ... D-Galactose (1-¹³C, 99%) microbiological/pyrogen tested. Item No.CLM-744-MPT-PK ... CIL) offers product CLM-744-1 D-Galactose (1-¹³C, 99%) ...
First described in a variant patient in 1935 by Mason and Turner, galactose-1-phosphate uridyltransferase (GALT) deficiency is ... Uridine diphosphate (UDP) galactose-4-epimerase epimerizes UDP galactose to UDP glucose and is also uncommon. [13] ... Galactose-1-Phosphate Uridyltransferase Deficiency (Galactosemia) * Sections Galactose-1-Phosphate Uridyltransferase Deficiency ... Galactokinase converts galactose to galactose-1-phosphate and is not a common deficiency. ...
US-3753725-A chemical patent summary.
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... from the D-mannose/L-galactose (Smirnoff-Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. The kinetic ... from the D-mannose/L-galactose (Smirnoff-Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. The kinetic ... from the D-mannose/L-galactose (Smirnoff-Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. The kinetic ... from the D-mannose/L-galactose (Smirnoff-Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. The kinetic ...
Simultaneous and rate-coordinated conversion of lignocellulose derived glucose, xylose, arabinose, mannose, and galactose into ... and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification and co- ... and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification and co- ... and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification and co- ...
2-Amino-3-deoxy-D-galactose Hydrochloride, D(+)-Galactosamine hydrochloride, D-Chondrosamine hydrochloride with the InChIKey ... 2-Amino-3-deoxy-D-galactose Hydrochloride, D(+)-Galactosamine hydrochloride, D-Chondrosamine hydrochloride; LC-ESI-QQ; MS2. ... CH$NAME: 2-Amino-3-deoxy-D-galactose Hydrochloride. CH$NAME: D(+)-Galactosamine hydrochloride. CH$NAME: D-Chondrosamine ... RECORD_TITLE: 2-Amino-3-deoxy-D-galactose Hydrochloride, D(+)-Galactosamine hydrochloride, D-Chondrosamine hydrochloride; LC- ...
The oxidation of D-glucose and D-galactose is catalyzed at a comparable rate (cf. EC 1.1.1.119 and EC 1.1.1.120). ... The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative ...
We offer the best-in-class Neoscreen Galactose kit worldwide. ... We offer High quality Neoscreen Galactose newborn screening kit ... Galactose-1-phosphate from dried blood spot followed by enzymatic conversion of Galactose-1-phosphate & Galactose. Two kinds of ... After extraction Galactose-1-phosphate converts to Galactose in a reaction catalyst by alkaline phophatase enzyme Then this ... Labsystems Diagnostics NeoScreen Galactose kit is intended for the quantification of Galactose. present in blood samples dried ...
C1GALT1 transfers Galactose to the Tn antigen forming Core 1 glycoproteins (T antigens) Stable Identifier ... C1GALT1 transfers Galactose to the Tn antigen forming Core 1 glycoproteins (T antigens) (Homo sapiens) ... C1GALT1 transfers Galactose to the Tn antigen forming Core 1 glycoproteins (T antigens) (Bos taurus) ... C1GALT1 transfers Galactose to the Tn antigen forming Core 1 glycoproteins (T antigens) (Caenorhabditis elegans) ...
Ling C . Effects of purslane herb on stress ability of aging mice induced by D-galactose[J]. Zhong Xi Yi Jie He Xue Bao, 2004,2 ... Effect of Liriope platyphylla total saponin on learning, memory and metabolites in aging mice induced by D-galactose Tao Jiang1 ... Effect of Liriope platyphylla total saponin on learning, memory and metabolites in aging mice induced by D-galactose. Journal ... LPTS could improve the memory of aging mice induced by D-galactose, promote its body weight, and increase the thymus and spleen ...
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Caramelization What is Caramelization? Caramelization is a complex group of reactions that take place when sugars, either dry or in concentrated aqueous solutions, are subjected to high temperatures to form unique brown colors and flavors in baked products and other food systems. Similar to Maillard reactions, caramelization is a distinct non-enzymatic browning [...]. ...
Galactose. French:. Galactose. Spanish:. Galactosa. Therapeutical categories:. Diagnostic agent, liver function. Pharmaceutic ... Galactose (USAN). This content is only available to registered users. If youre visiting this website the first time and would ...
Enzytec™ Liquid D-Galactose 0,01 €. Enzytec™ Liquid D-Galactose is an enzymatic assay for D-Galactose in foodstuff and other ... Enzytec™ Liquid Lactose/D-Galactose 0,01 €. Enzytec™ Liquid Lactose/D-Galactose is an enzymatic assay for Lactose / D-Galactose ... RIDA®CUBE D-Galactose 0,01 €. Enzymatic method for the determination of D-Galactose in food products and other sample materials ... RIDA®CUBE Lactose/D-Galactose 0,01 €. UV test for the determination of lactose / D-galactose (without differentiation) in food ...
Immune injury contributes to age-dependent SVD through the interaction of galactose α 1,3 galactose (Gal) a dominant xenogeneic ... Physical equivalency of wild type and Galactose α 1,3 Galactose free porcine pericardium; a new source material for ... Physical equivalency of wild type and Galactose α 1,3 Galactose free porcine pericardium; a new source material for ... Humans make high levels of antibody to carbohydrates with terminal galactose α 1,3 galactose (Gal) modifications. This Gal ...
At Team Galactose, were proud to announce, that were ready to open Pre-Orders for Galactose: Pastries in Space on KICKSTARTR. ... Jeskimo made an awesome lets play video of Galactose, please check it out! If anyone else makes a Galactose Lets Play video, ... Team Galactoses MAGFest Booth Overall, our booth had a pretty sweet setup and a pretty awesome location - a corner with a lot ... In that interval, a number of things have happened; We went to MAGFest 2014, we saw a lets play video of Galactose, we ...
The cause is a deficiency of galactose-1-phosphate-uridyltransferase, which metabolizes galactose-1-phosphate to UDP-galactose ... which catalyzes the conversion of galactose to galactose-1-phosphate. The ingested galactose cannot be metabolized in the ... Uridyl diphosphate galactose-4-epimerase deficiency[edit , edit source]. Uridyl diphosphate galactose-4-epimerase deficiency is ... Galactose crosses the placenta and the child may be exposed to galactose intrauterine. Therefore, mothers who have familiar ...
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  • Galactosemia is an inability to properly break down galactose due to a genetically inherited mutation in one of the enzymes in the Leloir pathway. (wikipedia.org)
  • Dietary galactose restriction does not appear to be necessary or beneficial in patients with Duarte D-2 variant galactosemia. (medscape.com)
  • Classical galactosemia can be demonstrated by increased concentrations of galacticol in urine and galactose-1-phosphate in erythrocytes. (wikilectures.eu)
  • Whether dietary galactose restriction is necessary or beneficial for patients with Duarte variant galactosemia is unknown. (medscape.com)
  • The enzymes are listed in the order of the metabolic pathway: galactokinase (GALK), galactose-1-phosphate uridyltransferase (GALT), and UDP-galactose-4'-epimerase (GALE). (wikipedia.org)
  • [ 9 ] Both patients probably had galactose-1-phosphate uridyltransferase (GALT) deficiency, which is the most common enzyme deficiency that causes hypergalactosemia. (medscape.com)
  • Individuals with GALT deficiency manifest abnormal galactose tolerance. (medscape.com)
  • Galactose-1-phosphate uridyltransferase is a blood test that measures the level of a substance called GALT, which helps break down milk sugars in your body. (mountsinai.org)
  • Comment: In the Leloir pathway, galactokinase (galK) forms galactose 1-phosphate, a uridyltransferase (galT) uses glucose 1-phosphate to form UDP-galactose, an epimerase (galE) forms UDP-glucose, and this is converted to glucose 1-phosphate by the same uridyltransferase. (lbl.gov)
  • Next, the enzyme galactose 1-phosphate uridyltransferase (GALT) converts galactose 1-phosphate to UDP-galactose which is finally converted to UDP-glucose via the enzyme UDP galactose-4′-epimerase (GALE). (theiopn.com)
  • Glucose-galactose malabsorption is a condition in which the body cannot take in (absorb) the sugars glucose and galactose, which primarily results in severe diarrhea. (medlineplus.gov)
  • The signs and symptoms of glucose-galactose malabsorption appear early in life when affected infants are fed breast milk or regular infant formulas. (medlineplus.gov)
  • Mutations in the SLC5A1 gene cause glucose-galactose malabsorption. (medlineplus.gov)
  • however, other proteins in the kidneys are able to absorb enough glucose into the bloodstream, so that glucosuria is mild, if present at all, in people with glucose-galactose malabsorption. (medlineplus.gov)
  • As the tablet coat contains sucrose (41.2 mg), patients with rare hereditary problems of fructose intolerance, glucose-galactose malabsorption or sucrase- isomaltase insufficiency should not take Buscopan Tablets. (janusinfo.se)
  • 3. lactose intolerance, lactase deficiency, glucose-galactose malabsorption. (who.int)
  • Galactose (/ɡəˈlæktoʊs/, galacto- + -ose, "milk sugar"), sometimes abbreviated Gal, is a monosaccharide sugar that is about as sweet as glucose, and about 65% as sweet as sucrose. (wikipedia.org)
  • Galactose is a monosaccharide. (wikipedia.org)
  • D-Galactose is a simple monosaccharide that serves as an energy source and as an essential component of glycolipids and glycoproteins. (rspharmchem.com)
  • Galactose is a naturally occurring monosaccharide that forms the disaccharide lactose when combined with glucose (another monosaccharide) 6 . (drugbank.com)
  • Galactose is a simple sugar and a monosaccharide. (pediaa.com)
  • D-galactose is a reducing monosaccharide which, if systemically exposed, causes accelerated senescence in several organs and is widely being used as an ideal agent to induce brain aging in animal models. (bmrat.org)
  • Therefore, the present monosaccharide β-galactose derivative can be used as a receptor for CT as an alternative to CT-specific antibodies or pentasaccharide ganglioside GM 1 , most widely used in conventional CT assays. (elsevierpure.com)
  • Galactokinase converts galactose to galactose-1-phosphate and is not a common deficiency. (medscape.com)
  • Galactose is a C-4 epimer of glucose and is catalyzed to glucose-1-phosphate by galactokinase, the rate-limiting step of metabolism for galactose exclusively in the liver [ 5 , 6 ]. (hindawi.com)
  • It is due to a lack of galactokinase, which catalyzes the conversion of galactose to galactose-1-phosphate. (wikilectures.eu)
  • To achieve this, galactose is firstly phosphorylated (a phosphate molecule is attached) to become galactose 1-phosphate via the enzyme galactokinase (GALK). (theiopn.com)
  • The hydrolysis of lactose to glucose and galactose is catalyzed by the enzymes lactase and β-galactosidase. (wikipedia.org)
  • Subsequently, when lactose or small amounts of free galactose found in various common dairy products (and other foods) are consumed, the hydrolysis of lactose to glucose and galactose occurs and galactose is itself further metabolized to generate glucose 6 . (drugbank.com)
  • Without this substance, the body cannot break down galactose, and the substance builds up in the blood. (mountsinai.org)
  • Since the metabolism of galactose is dependent on liver blood flow and hepatic functional mass, further studies are needed. (hindawi.com)
  • Named after the Nobel Prize winning biochemist Luis Leloir, the Leloir pathway, is the main pathway for the metabolism of galactose within the body and has been thought to occur exclusively within the liver. (theiopn.com)
  • The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. (expasy.org)
  • Finding step pgmA for D-galactose catabolism in Acidovorax sp. (lbl.gov)
  • The cause is a deficiency of galactose-1-phosphate-uridyltransferase, which metabolizes galactose-1-phosphate to UDP-galactose. (wikilectures.eu)
  • Uridyl diphosphate galactose-4-epimerase deficiency is a rare AR inherited disease , indicated by uridyldiphosphate galactose-4-epimerase deficiency. (wikilectures.eu)
  • The above mechanisms for galactose metabolism are necessary because the human body cannot directly convert galactose into energy, and must first go through one of these processes in order to utilize the sugar. (wikipedia.org)
  • caused by inherited deficiencies in enzymes that convert galactose to glucose. (msdmanuals.com)
  • Galactose metabolism, which converts galactose into glucose, is carried out by the three principal enzymes in a mechanism known as the Leloir pathway. (wikipedia.org)
  • The Leloir pathway consists of the latter stage of a two-part process that converts β-D-galactose to UDP-glucose. (wikipedia.org)
  • Here we describe the first crystal structure for an L-galactose dehydrogenase [Spinacia oleracea GDH (SoGDH) from spinach], from the D-mannose/L-galactose (Smirnoff-Wheeler) pathway which converts L-galactose into L-galactono-1,4-lactone. (edu.pe)
  • The tyrosyl radical, which directly coordinates to the copper ion center, has recently been found in the active sites of galactose oxidase (GAO) and glyoxal oxidase (GLO). (ewha.ac.kr)
  • The organic, acid and base soluble components of the above fractions were then used to demonstrate inhibition of the metal dependent enzyme, galactose oxidase. (cdc.gov)
  • This study showed a simultaneous and rate-coordinated conversion of lignocellulose derived glucose, xylose, arabinose, mannose, and galactose into D-lactic acid by adaptively evolved Pediococcus acidilactici ZY271 by simultaneous saccharification and co-fermentation (SSCF) of wheat straw. (lu.se)
  • As an example, glucose-based carbohydrates appear effective in restoring muscle glycogen but are less effective in restoring liver glycogen compared to other sugars such as fructose and galactose (Gonzalez et al. (theiopn.com)
  • Sugar is one of the simple forms of carbohydrates which contains mono-saccharides, such as fructose (found in fruits) and galactose (found in milk products), and disaccharides (carbohydrates with two sugars), such as sucrose (table sugar) and lactose (from dairy) (1). (who.int)
  • Many speculate that it is for this reason that a pathway for rapid conversion from galactose to glucose has been highly conserved among many species. (wikipedia.org)
  • and finally, UDP galactose-4'-epimerase (GALE) interconverts UDP-galactose and UDP-glucose, thereby completing the pathway. (wikipedia.org)
  • The ingested galactose cannot be metabolized in the normal way, so it is metabolized by the aldose-reductase pathway to the galacticol side. (wikilectures.eu)
  • D-Galactose contributes to energy metabolism via its conversion to glucose by the enzymes that constitute the Leloir pathway. (rspharmchem.com)
  • Regardless, although it is predominantly used as a pathway to generate glucose fuel for the human body, galactose is involved as an ingredient in some commonly used vaccines and non-prescription products. (drugbank.com)
  • Overview: Galactose utilization in GapMind is based on MetaCyc pathways lactose and galactose degradation I via tagatose 6-phosphate ( link ), the Leloir pathway via UDP-galactose ( link ), and the oxidative pathway via D-galactonate ( link ). (lbl.gov)
  • Comment: The tagatose 6-phosphate pathway involves the isomerization of galactose 6-phosphate to tagatose-6-phosphate (by lacAB), phosphorylation to tagatose 1,6-bisphosphate (by lacC), and an aldolase. (lbl.gov)
  • Moreover, the researchers measured the expression of key enzymes involved in the Leloir pathway (see below) to determine whether skeletal muscle has the capacity of directly metabolising galactose. (theiopn.com)
  • The word galactose was coined by Charles Weissman in the mid-19th century and is derived from Greek γαλακτος, galaktos, (of milk) and the generic chemical suffix for sugars -ose. (wikipedia.org)
  • These foods contain glucose, galactose, and another sugar called lactose that gets broken down into these two sugars. (medlineplus.gov)
  • GALM (glactose mutorotase, aldose1-epimerase) catalyzes the interconversion of the alpha and the beta anomers of hexose sugars like glucose and galactose and is not common. (medscape.com)
  • Galactose is part of lactose, the sugars in milk and dairy products. (hollandandbarrett.com)
  • Galactose is another name for lactose sugars. (hollandandbarrett.com)
  • Glucose and Galactose are very important simple sugars as monosaccharides as well as polysaccharides , which are formed after their polymerization. (pediaa.com)
  • Although various combinations of sugars have been studied, galactose (one of the sugars found within lactose) has received little attention, with its effect on muscle glycogen resynthesis yet to be investigated. (theiopn.com)
  • This suggests that the synthesis of galactose is supplemented by direct uptake and of use of plasma galactose when present. (wikipedia.org)
  • Salmonella typhimurium gal E mutants used to produce the vaccine are effectively avirulent and highly protective but lack the specific UDP-galactose 4-epimerase enzyme which allows for the normal synthesis of UDP-galactose from UDP-glucose 12 . (drugbank.com)
  • Galactose exists in both open-chain and cyclic form. (wikipedia.org)
  • Galactose can exist either in the open chain form or the cyclic form. (pediaa.com)
  • Galactan is a polymeric form of galactose found in hemicellulose, and forming the core of the galactans, a class of natural polymeric carbohydrates. (wikipedia.org)
  • Humans make high levels of antibody to carbohydrates with terminal galactose α 1,3 galactose (Gal) modifications. (ucl.ac.uk)
  • Glucose and galactose are carbohydrates. (pediaa.com)
  • Many metabolic disease specialists take a conservative approach and recommend galactose restriction in the first year of life when milk intake is highest, but this restriction is based primarily on theoretical concerns of galactose toxicity in infants with the Duarte D-2 variant. (medscape.com)
  • In normal diets, most galactose comes from the breakdown ( metabolism ) of lactose, which is found in milk and dairy products. (mountsinai.org)
  • The present study examined the efficiency of goat milk supplementation on memory performance in a D-galactose induced aging rat model. (bmrat.org)
  • Fifty-two male Sprague Dawley rats were randomly divided into four groups: 1) control group, 2) goat milk treated group, 3) D-galactose treated group, and 4) goat milk plus D-galactose treated group. (bmrat.org)
  • D-galactose (120 mg/kg subcutaneously) and/or goat milk (1 g/kg orally) were administered continuously for six weeks, preceded and followed by novel object recognition and T-maze tests. (bmrat.org)
  • 0.0001) short-term, long-term and spatial memory performance of the D-galactose plus goat milk treated group, compared to the D-galactose treated group. (bmrat.org)
  • Alpha-gal syndrome (AGS) is an emerging, tick bite-associated allergic condition characterized by a potentially life-threatening immunoglobulin E (IgE)-mediated hypersensitivity to galactose-alpha-1,3-galactose (alpha-gal), an oligosaccharide found in most nonprimate mammalian tissue and products derived from these mammals, such as milk, other dairy products, and some pharmaceutical products. (medscape.com)
  • Lactose is a disaccharide of galactose plus glucose. (wikipedia.org)
  • Ige Antibody Laboratories manufactures the serum alpha galactose ige antibody reagents distributed by Genprice. (nfkb-p65.org)
  • Immune injury contributes to age-dependent SVD through the interaction of galactose α 1,3 galactose (Gal) a dominant xenogeneic antigen present on commercial BHVs and universally abundant human anti-Gal antibody. (ucl.ac.uk)
  • Galactose contributes to the formation of some disaccharides such as Lactose (Glucose + Galactose) and Galactan (composed of Galactose). (pediaa.com)
  • Uridine diphosphate (UDP) galactose-4-epimerase epimerizes UDP galactose to UDP glucose and is also uncommon. (medscape.com)
  • During infancy, but less so in childhood, these individuals may have elevated galactose metabolite levels. (medscape.com)
  • The initial stage is the conversion of β-D-galactose to α-D-galactose by the enzyme, mutarotase (GALM). (wikipedia.org)
  • The Serum Alpha Galactose Ige Antibody reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (nfkb-p65.org)
  • D-Galactose is also known as brain sugar since it is a component of glycoproteins (oligosaccharide-protein compounds) found in nerve tissue. (wikipedia.org)
  • MIM:610555) mediates the transfer of Galactose (Gal) from UDP galactose to single O-linked GalNAc residues (Tn antigens) to form Core 1 structures on glycoproteins. (reactome.org)
  • Enzytec™ Liquid D-Galactose is an enzymatic assay for D-Galactose in foodstuff and other sample materials. (biotica.gr)
  • Enzytec™ Liquid Lactose/D-Galactose is an enzymatic assay for Lactose / D-Galactose in foodstuff and other sample materials (without differentiation). (biotica.gr)
  • Enzymatic method for the determination of D-Galactose in food products and other sample materials (UV-method). (biotica.gr)
  • Galactose is present in dairy products, fruits, and vegetables. (msdmanuals.com)
  • Berry GT, Segal S and Gitzelmann R. Disorders of Galactose Metabolism. (medscape.com)
  • Monocyte galactose/N-acetylgalactosamine-specific C-type lectin receptor stimulant immunotherapy of an experimental glioma. (dovepress.com)
  • A peptide mimetic of a ligand for the galactose/N-acetylgalactosamine-specific C-type lectin receptors (GCLR) exhibited monocyte-stimulating activity, but did not extend survival when applied alone against a syngeneic murine malignant glioma. (dovepress.com)
  • A galactose molecule linked with a glucose molecule forms a lactose molecule. (wikipedia.org)
  • The oxidation of D-glucose and D-galactose is catalyzed at a comparable rate (cf. (expasy.org)
  • The galactose single-point (GSP) test assesses functioning liver mass by measuring the galactose concentration in the blood 1 hour after its administration. (hindawi.com)
  • The galactose single point (GSP) test is one novel method of assessing residual liver function. (hindawi.com)
  • The ability of hepatocytes to metabolize galactose depends on total functioning liver mass and blood flow through the liver [ 7 ]. (hindawi.com)
  • Glucose is more stable than galactose and is less susceptible to the formation of nonspecific glycoconjugates, molecules with at least one sugar attached to a protein or lipid. (wikipedia.org)
  • Galactose is less stable. (pediaa.com)
  • Galactose has been used in trials studying the treatment and diagnosis of Hepatitis C, Hepatic Cancer, Wilsons Disease, Diabetic Macular Oedema, and Focal Segmental Glomerulosclerosis, among others. (drugbank.com)
  • Regardless, the mutant's epimerase defect ultimately results in the accumulation of such intermediary products like galactose 1-phosphate and UDP-galactose, which consequently causes lysis of the mutant cells. (drugbank.com)
  • Alpha-gal syndrome (AGS) is an emerging, tick bite-associated allergic condition characterized by a potentially life-threatening immunoglobulin E (IgE)-mediated hypersensitivity to galactose-alpha-1,3-galactose (alpha-gal), an oligosaccharide found in most nonprimate mammalian meat and products derived from these mammals. (medscape.com)

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