A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
The largest of the three pairs of SALIVARY GLANDS. They lie on the sides of the FACE immediately below and in front of the EAR.
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
Enzymes that catalyze the endohydrolysis of 1,4-alpha-glycosidic linkages in STARCH; GLYCOGEN; and related POLYSACCHARIDES and OLIGOSACCHARIDES containing 3 or more 1,4-alpha-linked D-glucose units.
An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.
INFLAMMATION of the PANCREAS. Pancreatitis is classified as acute unless there are computed tomographic or endoscopic retrograde cholangiopancreatographic findings of CHRONIC PANCREATITIS (International Symposium on Acute Pancreatitis, Atlanta, 1992). The two most common forms of acute pancreatitis are ALCOHOLIC PANCREATITIS and gallstone pancreatitis.
A specific decapeptide obtained from the skin of Hila caerulea, an Australian amphibian. Caerulein is similar in action and composition to CHOLECYSTOKININ. It stimulates gastric, biliary, and pancreatic secretion; and certain smooth muscle. It is used in paralytic ileus and as diagnostic aid in pancreatic malfunction.
One of two major pharmacologically defined classes of adrenergic receptors. The beta adrenergic receptors play an important role in regulating CARDIAC MUSCLE contraction, SMOOTH MUSCLE relaxation, and GLYCOGENOLYSIS.
An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.
The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.
An enzyme that hydrolyzes 1,6-alpha-glucosidic branch linkages in glycogen, amylopectin, and their beta-limit dextrins. It is distinguished from pullulanase (EC 3.2.1.41) by its inability to attack pullulan and by the feeble action of alpha-limit dextrins. It is distinguished from amylopectin 6-glucanohydrolase (EC 3.2.1.69) by its action on glycogen. With EC 3.2.1.69, it produces the activity called "debranching enzyme". EC 3.2.1.68.
A peptide, of about 33 amino acids, secreted by the upper INTESTINAL MUCOSA and also found in the central nervous system. It causes gallbladder contraction, release of pancreatic exocrine (or digestive) enzymes, and affects other gastrointestinal functions. Cholecystokinin may be the mediator of satiety.
The fluid containing digestive enzymes secreted by the pancreas in response to food in the duodenum.
An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.
Any of a group of polysaccharides of the general formula (C6-H10-O5)n, composed of a long-chain polymer of glucose in the form of amylose and amylopectin. It is the chief storage form of energy reserve (carbohydrates) in plants.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
An octapeptide hormone present in the intestine and brain. When secreted from the gastric mucosa, it stimulates the release of bile from the gallbladder and digestive enzymes from the pancreas.
A subclass of alpha-amylase ISOENZYMES that are secreted into SALIVA.
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.
Also known as CD104 antigen, this protein is distinguished from other beta integrins by its relatively long cytoplasmic domain (approximately 1000 amino acids vs. approximately 50). Five alternatively spliced isoforms have been described.
Chymotrypsinogen is a zymogen, specifically an inactive precursor form of the enzyme chymotrypsin, which is produced in the pancreas and activated in the small intestine to help digest proteins by cleaving specific peptide bonds.
This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.
Integrin beta chains combine with integrin alpha chains to form heterodimeric cell surface receptors. Integrins have traditionally been classified into functional groups based on the identity of one of three beta chains present in the heterodimer. The beta chain is necessary and sufficient for integrin-dependent signaling. Its short cytoplasmic tail contains sequences critical for inside-out signaling.
A 44-kDa highly glycosylated plasma protein that binds phospholipids including CARDIOLIPIN; APOLIPOPROTEIN E RECEPTOR; membrane phospholipids, and other anionic phospholipid-containing moieties. It plays a role in coagulation and apoptotic processes. Formerly known as apolipoprotein H, it is an autoantigen in patients with ANTIPHOSPHOLIPID ANTIBODIES.
Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.
A condition with abnormally elevated level of AMYLASES in the serum. Hyperamylasemia due to PANCREATITIS or other causes may be differentiated by identifying the amylase isoenzymes.
The major component (about 80%) of the PANCREAS composed of acinar functional units of tubular and spherical cells. The acinar cells synthesize and secrete several digestive enzymes such as TRYPSINOGEN; LIPASE; AMYLASE; and RIBONUCLEASE. Secretion from the exocrine pancreas drains into the pancreatic ductal system and empties into the DUODENUM.
An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-2 receptors are more sensitive to EPINEPHRINE than to NOREPINEPHRINE and have a high affinity for the agonist TERBUTALINE. They are widespread, with clinically important roles in SKELETAL MUSCLE; LIVER; and vascular, bronchial, gastrointestinal, and genitourinary SMOOTH MUSCLE.
Bethanechol compounds are parasympathomimetic agents that directly stimulate muscarinic receptors, primarily used to treat urinary retention and nonobstructive bladder dysfunction by increasing bladder contractility and decreasing post-void residual volume.
Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The amount of a substance secreted by cells or by a specific organ or organism over a given period of time; usually applies to those substances which are formed by glandular tissues and are released by them into biological fluids, e.g., secretory rate of corticosteroids by the adrenal cortex, secretory rate of gastric acid by the gastric mucosa.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation.
Integrin beta-1 chains which are expressed as heterodimers that are noncovalently associated with specific alpha-chains of the CD49 family (CD49a-f). CD29 is expressed on resting and activated leukocytes and is a marker for all of the very late activation antigens on cells. (from: Barclay et al., The Leukocyte Antigen FactsBook, 1993, p164)
A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.
Isopropyl analog of EPINEPHRINE; beta-sympathomimetic that acts on the heart, bronchi, skeletal muscle, alimentary tract, etc. It is used mainly as bronchodilator and heart stimulant.
Disease having a short and relatively severe course.
Drugs that selectively bind to and activate beta-adrenergic receptors.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-1 receptors are equally sensitive to EPINEPHRINE and NOREPINEPHRINE and bind the agonist DOBUTAMINE and the antagonist METOPROLOL with high affinity. They are found in the HEART, juxtaglomerular cells, and in the central and peripheral nervous systems.
A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. (USAN and the USP Dictionary of Drug Names, 1994, p597)
Established cell cultures that have the potential to propagate indefinitely.
A dextrodisaccharide from malt and starch. It is used as a sweetening agent and fermentable intermediate in brewing. (Grant & Hackh's Chemical Dictionary, 5th ed)
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.
The rate dynamics in chemical or physical systems.
Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.
Pathological processes of the PANCREAS.
Oligosaccharides containing three monosaccharide units linked by glycosidic bonds.
A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
One of the ESTROGEN RECEPTORS that has greater affinity for ISOFLAVONES than ESTROGEN RECEPTOR ALPHA does. There is great sequence homology with ER alpha in the DNA-binding domain but not in the ligand binding and hinge domains.
Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.
A subclass of alpha-amylase ISOENZYMES that are secreted into PANCREATIC JUICE.
A subtype of transforming growth factor beta that is synthesized by a wide variety of cells. It is synthesized as a precursor molecule that is cleaved to form mature TGF-beta 1 and TGF-beta1 latency-associated peptide. The association of the cleavage products results in the formation a latent protein which must be activated to bind its receptor. Defects in the gene that encodes TGF-beta1 are the cause of CAMURATI-ENGELMANN SYNDROME.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A slowly hydrolyzed CHOLINERGIC AGONIST that acts at both MUSCARINIC RECEPTORS and NICOTINIC RECEPTORS.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The beta-3 adrenergic receptors are the predominant beta-adrenergic receptor type expressed in white and brown ADIPOCYTES and are involved in modulating ENERGY METABOLISM and THERMOGENESIS.
The relationship between the dose of an administered drug and the response of the organism to the drug.

Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution. (1/94)

The crystal structure of beta-amylase from Bacillus cereus var. mycoides was determined by the multiple isomorphous replacement method. The structure was refined to a final R-factor of 0.186 for 102,807 independent reflections with F/sigma(F) > or = 2.0 at 2.2 A resolution with root-mean-square deviations from ideality in bond lengths, and bond angles of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds into three domains; the first one is the N-terminal catalytic domain with a (beta/alpha)8 barrel, the second one is the excursion part from the first one, and the third one is the C-terminal domain with two almost anti-parallel beta-sheets. The active site cleft, including two putative catalytic residues (Glu172 and Glu367), is located on the carboxyl side of the central beta-sheet in the (beta/alpha)8 barrel, as in most amylases. The active site structure of the enzyme resembles that of soybean beta-amylase with slight differences. One calcium ion is bound per molecule far from the active site. The C-terminal domain has a fold similar to the raw starch binding domains of cyclodextrin glycosyltransferase and glucoamylase.  (+info)

The evolution of starch-binding domain. (2/94)

Amylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain the starch-binding domain (SBD) positioned almost exclusively at the C-terminus. Detailed analysis of all available SBD sequences from 43 different amylases revealed its independent evolutionary behaviour with regard to the catalytic domains. In the evolutionary tree based on sequence alignment of the SBDs, taxonomy is respected so that fungi and actinomycetes form their own separate parts surrounded by bacteria that are also clustered according to taxonomy. The only known N-terminal SBD from Rhizopus oryzae glucoamylase is on the longest branch separated from all C-terminal SBDs. The 3-dimensional (3-D) structures of fungal glucoamylase and bacterial CGTase SBDs are compared and used to discuss the interesting SBD evolution.  (+info)

Prediction of protein cleavage sites by the barley cysteine endoproteases EP-A and EP-B based on the kinetics of synthetic peptide hydrolysis. (3/94)

Hordeins, the natural substrates of barley (Hordeum vulgare) cysteine endoproteases (EPs), were isolated as protein bodies and degraded by purified EP-B from green barley malt. Cleavage specificity was determined by synthesizing internally quenched, fluorogenic tetrapeptide substrates of the general formula 2-aminobenzoyl-P(2)-P(1)-P(1)'-P(2)' 1-tyrosine(NO(2))-aspartate. The barley EPs preferred neutral amino acids with large aliphatic and nonpolar (leucine, valine, isoleucine, and methionine) or aromatic (phenylalanine, tyrosine, and tryptophan) side chains at P(2), and showed less specificity at P(1), although asparagine, aspartate, valine, and isoleucine were particularly unfavorable. Peptides with proline at P(1) or P(1)' were extremely poor substrates. Cleavage sites with EP-A and EP-B preferred substrate sequences are found in hordeins, their natural substrates. The substrate specificity of EP-B with synthetic peptides was used successfully to predict the cleavage sites in the C-terminal extension of barley beta-amylase. When all of the primary cleavage sites in C hordein, which occur mainly in the N- and C-terminal domains, were removed by site-directed mutagenesis, the resulting protein was degraded 112 times more slowly than wild-type C hordein. We suggest that removal of the C hordein terminal domains is necessary for unfolding of the beta-reverse turn helix of the central repeat domain, which then becomes more susceptible to proteolytic attack by EP-B.  (+info)

Water stress enhances beta-amylase activity in cucumber cotyledons. (4/94)

Cotyledons detached from 4-d-old cucumber (Cucumis sativus L.) seedlings were subjected to water stress (air-drying or PEG-treatment) to examine the effects of the stress on carbohydrate metabolism. Amylolytic activity in the cotyledon was increased about 6-fold by water stress within 1 d. The substrate specificity and the action pattern indicated that beta-amylase is responsible for the activity. Activities of azocaseinase, malate dehydrogenase and triose-phosphate isomerase were not affected by water stress, indicating that the effect of the stress on beta-amylase is rather specific. Cycloheximide-treatment strongly reduced the enhancement of beta-amylase activity. The hypocotyl of cucumber seedlings also exhibited an increase in the enzyme activity when subjected to water stress. The major free sugars in cucumber cotyledons were glucose, fructose, maltose, and sucrose; sucrose being the most abundant. Sucrose content in excised, unstressed cotyledons increased markedly during the incubation. Changes in other free sugars were small compared with that of sucrose. Starch also accumulated in unstressed cotyledons. In stressed cotyledons more sucrose and less starch accumulated than in unstressed ones. Such results were discussed in relation to the enhancement of beta-amylase activity.  (+info)

Polymorphism in rice amylases at an early stage of seed germination. (5/94)

A polymorphism in rice amylases at an early stage of seed germination is analyzed by zymogram. In non-glutinous cultivars of rice, alpha-amylase isozymes are mainly confirmed in germinating seeds. However, in glutinous cultivars, beta-amylase isozymes, which are not confirmed in nonglutinous cultivars, make up the major part of the total amylase activity and the expression of alpha-amylases are repressed.  (+info)

Molecular mimicry of substrate oxygen atoms by water molecules in the beta-amylase active site. (6/94)

Soybean beta-amylase (EC 3.2.1.2) has been crystallized both free and complexed with a variety of ligands. Four water molecules in the free-enzyme catalytic cleft form a multihydrogen-bond network with eight strategic residues involved in enzyme-ligand hydrogen bonds. We show here that the positions of these four water molecules are coincident with the positions of four potential oxygen atoms of the ligands within the complex. Some of these waters are displaced from the active site when the ligands bind to the enzyme. How many are displaced depends on the shape of the ligand. This means that when one of the four positions is not occupied by a ligand oxygen atom, the corresponding water remains. We studied the functional/structural role of these four waters and conclude that their presence means that the conformation of the eight side chains is fixed in all situations (free or complexed enzyme) and preserved from unwanted or forbidden conformational changes that could hamper the catalytic mechanism. The water structure at the active pocket of beta-amylase is therefore essential for providing the ligand recognition process with plasticity. It does not affect the protein active-site geometry and preserves the overall hydrogen-bonding network, irrespective of which ligand is bound to the enzyme. We also investigated whether other enzymes showed a similar role for water. Finally, we discuss the potential use of these results for predicting whether water molecules can mimic ligand atoms in the active center.  (+info)

Activities of starch hydrolytic enzymes and sucrose-phosphate synthase in the stems of rice subjected to water stress during grain filling. (7/94)

To understand the effect of water stress on the remobilization of prestored carbon reserves, the changes in the activities of starch hydrolytic enzymes and sucrose-phosphate synthase (SPS) in the stems of rice (Oryza sativa L.) during grain filling were investigated. Two rice cultivars, showing high lodging-resistance and slow remobilization, were grown in the field and subjected to well-watered (WW, psi(soil)=0) and water-stressed (WS, psi(soil)=-0.05 MPa) treatments 9 d after anthesis (DAA) till maturity. Leaf water potentials of both cultivars markedly decreased during the day as a result of WS treatment, but completely recovered by early morning. WS treatment accelerated the reduction of starch in the stems, promoted the reallocation of prefixed (14)C from the stems to grains, shortened the grain filling period, and increased the grain filling rate. More soluble sugars including sucrose were accumulated in the stems under WS than under WW treatments. Both alpha- and beta-amylase activities were enhanced by the WS, with the former enhanced more than the latter, and were significantly correlated with the concentrations of soluble sugars in the stems. The other two possible starch-breaking enzymes, alpha-glucosidase and starch phosphorylase, showed no significant differences in the activities between the WW and WS treatments. Water stress also increased the SPS activity that is responsible for sucrose production. Both V(limit) and V(max), the activities of the enzyme at limiting and saturating substrate concentrations, were enhanced and the activation state (V(limit)/V(max)) was also increased as a result of the more significant enhancement of V(limit). The enhanced SPS activity was closely correlated with an increase of sucrose accumulation in the stems. The results suggest that the fast hydrolysis of starch and increased carbon remobilization were attributed to the enhanced alpha-amylase activity and the high activation state of SPS when the rice was subjected to water stress.  (+info)

Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic beta-amylase from Calystegia sepium (hedge bindweed) rhizomes. (8/94)

An abundant catalytically active beta-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant beta-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the beta-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome beta-amylase is a cytoplasmic vegetative storage protein.  (+info)

Amylases are enzymes that break down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, glucose, and maltotriose. There are several types of amylases found in various organisms, including humans.

In humans, amylases are produced by the pancreas and salivary glands. Pancreatic amylase is released into the small intestine where it helps to digest dietary carbohydrates. Salivary amylase, also known as alpha-amylase, is secreted into the mouth and begins breaking down starches in food during chewing.

Deficiency or absence of amylases can lead to difficulties in digesting carbohydrates and may cause symptoms such as bloating, diarrhea, and abdominal pain. Elevated levels of amylase in the blood may indicate conditions such as pancreatitis, pancreatic cancer, or other disorders affecting the pancreas.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

The parotid gland is the largest of the major salivary glands. It is a bilobed, accessory digestive organ that secretes serous saliva into the mouth via the parotid duct (Stensen's duct), located near the upper second molar tooth. The parotid gland is primarily responsible for moistening and lubricating food to aid in swallowing and digestion.

Anatomically, the parotid gland is located in the preauricular region, extending from the zygomatic arch superiorly to the angle of the mandible inferiorly, and from the masseter muscle anteriorly to the sternocleidomastoid muscle posteriorly. It is enclosed within a fascial capsule and has a rich blood supply from the external carotid artery and a complex innervation pattern involving both parasympathetic and sympathetic fibers.

Parotid gland disorders can include salivary gland stones (sialolithiasis), infections, inflammatory conditions, benign or malignant tumors, and autoimmune diseases such as Sjögren's syndrome.

Interleukin-1 beta (IL-1β) is a member of the interleukin-1 cytokine family and is primarily produced by activated macrophages in response to inflammatory stimuli. It is a crucial mediator of the innate immune response and plays a key role in the regulation of various biological processes, including cell proliferation, differentiation, and apoptosis. IL-1β is involved in the pathogenesis of several inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and atherosclerosis. It exerts its effects by binding to the interleukin-1 receptor, which triggers a signaling cascade that leads to the activation of various transcription factors and the expression of target genes.

Alpha-amylases are a type of enzyme that breaks down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, maltotriose, and glucose. These enzymes catalyze the hydrolysis of alpha-1,4 glycosidic bonds in these complex carbohydrates, making them more easily digestible.

Alpha-amylases are produced by various organisms, including humans, animals, plants, and microorganisms such as bacteria and fungi. In humans, alpha-amylases are primarily produced by the salivary glands and pancreas, and they play an essential role in the digestion of dietary carbohydrates.

Deficiency or malfunction of alpha-amylases can lead to various medical conditions, such as diabetes, kidney disease, and genetic disorders like congenital sucrase-isomaltase deficiency. On the other hand, excessive production of alpha-amylases can contribute to dental caries and other oral health issues.

Beta-2 microglobulin (β2M) is a small protein that is a component of the major histocompatibility complex class I molecule, which plays a crucial role in the immune system. It is found on the surface of almost all nucleated cells in the body and is involved in presenting intracellular peptides to T-cells for immune surveillance.

β2M is produced at a relatively constant rate by cells throughout the body and is freely filtered by the glomeruli in the kidneys. Under normal circumstances, most of the filtrated β2M is reabsorbed and catabolized in the proximal tubules of the nephrons. However, when the glomerular filtration rate (GFR) is decreased, as in chronic kidney disease (CKD), the reabsorption capacity of the proximal tubules becomes overwhelmed, leading to increased levels of β2M in the blood and its subsequent appearance in the urine.

Elevated serum and urinary β2M levels have been associated with various clinical conditions, such as CKD, multiple myeloma, autoimmune disorders, and certain infectious diseases. Measuring β2M concentrations can provide valuable information for diagnostic, prognostic, and monitoring purposes in these contexts.

Pancreatitis is a medical condition characterized by inflammation of the pancreas, a gland located in the abdomen that plays a crucial role in digestion and regulating blood sugar levels. The inflammation can be acute (sudden and severe) or chronic (persistent and recurring), and it can lead to various complications if left untreated.

Acute pancreatitis often results from gallstones or excessive alcohol consumption, while chronic pancreatitis may be caused by long-term alcohol abuse, genetic factors, autoimmune conditions, or metabolic disorders like high triglyceride levels. Symptoms of acute pancreatitis include severe abdominal pain, nausea, vomiting, fever, and increased heart rate, while chronic pancreatitis may present with ongoing abdominal pain, weight loss, diarrhea, and malabsorption issues due to impaired digestive enzyme production. Treatment typically involves supportive care, such as intravenous fluids, pain management, and addressing the underlying cause. In severe cases, hospitalization and surgery may be necessary.

Ceruletide is a synthetic analog of the natural hormone cholecystokinin (CCK). It is a decapeptide with the following sequence: cyclo(D-Asp-Tic-Phe-Ser-Leu-Hand-Ala-Lys-Thr-Nle-NH2).

Ceruletide has several pharmacological actions, including stimulation of the release of digestive enzymes from the pancreas, contraction of the gallbladder and sphincter of Oddi, and inhibition of gastric acid secretion. It is used in clinical medicine for diagnostic purposes to test the motor function of the biliary tract and to diagnose gastrointestinal motility disorders.

Ceruletide has also been investigated as a potential treatment for certain conditions such as pancreatitis, gallstones, and intestinal obstruction, but its use is limited due to its side effects, which include nausea, vomiting, abdominal cramps, and diarrhea.

Adrenergic receptors are a type of G protein-coupled receptor that binds and responds to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Beta adrenergic receptors (β-adrenergic receptors) are a subtype of adrenergic receptors that include three distinct subclasses: β1, β2, and β3. These receptors are widely distributed throughout the body and play important roles in various physiological functions, including cardiovascular regulation, bronchodilation, lipolysis, and glucose metabolism.

β1-adrenergic receptors are primarily located in the heart and regulate cardiac contractility, chronotropy (heart rate), and relaxation. β2-adrenergic receptors are found in various tissues, including the lungs, vascular smooth muscle, liver, and skeletal muscle. They mediate bronchodilation, vasodilation, glycogenolysis, and lipolysis. β3-adrenergic receptors are mainly expressed in adipose tissue, where they stimulate lipolysis and thermogenesis.

Agonists of β-adrenergic receptors include catecholamines like epinephrine and norepinephrine, as well as synthetic drugs such as dobutamine (a β1-selective agonist) and albuterol (a non-selective β2-agonist). Antagonists of β-adrenergic receptors are commonly used in the treatment of various conditions, including hypertension, angina pectoris, heart failure, and asthma. Examples of β-blockers include metoprolol (a β1-selective antagonist) and carvedilol (a non-selective β-blocker with additional α1-adrenergic receptor blocking activity).

Integrin β3 is a subunit of certain integrin heterodimers, which are transmembrane receptors that mediate cell-cell and cell-extracellular matrix (ECM) adhesion. Integrin β3 combines with either integrin αv (to form the integrin αvβ3) or integrin αIIb (to form the integrin αIIbβ3). These integrins are involved in various cellular processes, including platelet aggregation, angiogenesis, and tumor metastasis.

Integrin αIIbβ3 is primarily expressed on platelets and mediates platelet aggregation by binding to fibrinogen, von Willebrand factor, and other adhesive proteins in the ECM. Integrin αvβ3 is widely expressed in various cell types and participates in diverse functions such as cell migration, proliferation, differentiation, and survival. It binds to a variety of ECM proteins, including fibronectin, vitronectin, and osteopontin, as well as to soluble ligands like vascular endothelial growth factor (VEGF) and transforming growth factor-β (TGF-β).

Dysregulation of integrin β3 has been implicated in several pathological conditions, such as thrombosis, atherosclerosis, tumor metastasis, and inflammatory diseases.

Saliva is a complex mixture of primarily water, but also electrolytes, enzymes, antibacterial compounds, and various other substances. It is produced by the salivary glands located in the mouth. Saliva plays an essential role in maintaining oral health by moistening the mouth, helping to digest food, and protecting the teeth from decay by neutralizing acids produced by bacteria.

The medical definition of saliva can be stated as:

"A clear, watery, slightly alkaline fluid secreted by the salivary glands, consisting mainly of water, with small amounts of electrolytes, enzymes (such as amylase), mucus, and antibacterial compounds. Saliva aids in digestion, lubrication of oral tissues, and provides an oral barrier against microorganisms."

Isoamylase is not a medical term per se, but rather a biochemical term used to describe an enzyme. Medically, it may be relevant in the context of certain medical conditions or treatments that involve carbohydrate metabolism. Here's a general definition:

Isoamylase (EC 3.2.1.68) is a type of amylase, a group of enzymes that break down complex carbohydrates, specifically starch and glycogen, into simpler sugars. Isoamylase is more precisely defined as an enzyme that hydrolyzes (breaks down) alpha-1,6 glucosidic bonds in isomaltose, panose, and dextrins, yielding mainly isomaltose and limit dextrin. It is found in various organisms, including bacteria, fungi, and plants. In humans, isoamylase is involved in the digestion of starch in the small intestine, where it helps convert complex carbohydrates into glucose for energy absorption.

Cholecystokinin (CCK) is a hormone that is produced in the duodenum (the first part of the small intestine) and in the brain. It is released into the bloodstream in response to food, particularly fatty foods, and plays several roles in the digestive process.

In the digestive system, CCK stimulates the contraction of the gallbladder, which releases bile into the small intestine to help digest fats. It also inhibits the release of acid from the stomach and slows down the movement of food through the intestines.

In the brain, CCK acts as a neurotransmitter and has been shown to have effects on appetite regulation, mood, and memory. It may play a role in the feeling of fullness or satiety after eating, and may also be involved in anxiety and panic disorders.

CCK is sometimes referred to as "gallbladder-stimulating hormone" or "pancreozymin," although these terms are less commonly used than "cholecystokinin."

Pancreatic juice is an alkaline fluid secreted by the exocrine component of the pancreas, primarily containing digestive enzymes such as amylase, lipase, and trypsin. These enzymes aid in the breakdown of carbohydrates, fats, and proteins, respectively, in the small intestine during the digestion process. The bicarbonate ions present in pancreatic juice help neutralize the acidic chyme that enters the duodenum from the stomach, creating an optimal environment for enzymatic activity.

Lipase is an enzyme that is produced by the pancreas and found in the digestive system of most organisms. Its primary function is to catalyze the hydrolysis of fats (triglycerides) into smaller molecules, such as fatty acids and glycerol, which can then be absorbed by the intestines and utilized for energy or stored for later use.

In medical terms, lipase levels in the blood are often measured to diagnose or monitor conditions that affect the pancreas, such as pancreatitis (inflammation of the pancreas), pancreatic cancer, or cystic fibrosis. Elevated lipase levels may indicate damage to the pancreas and its ability to produce digestive enzymes.

I'm happy to help! However, it seems there might be a bit of confusion here. Starch is not typically considered a medical term, but rather a nutritional and biochemical concept. Here's a brief explanation:

Starch is a complex carbohydrate that serves as the primary form of energy storage in plants. It is made up of long chains of glucose molecules and can be found in various foods such as grains, legumes, fruits, and vegetables. Amylase, an enzyme present in our saliva and digestive system, helps break down starch into simpler sugars during the digestion process so that our bodies can absorb them for energy.

I hope this clarifies any confusion! If you have any other questions or need further information on a medical topic, please don't hesitate to ask.

Transforming Growth Factor-beta (TGF-β) is a type of cytokine, which is a cell signaling protein involved in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). TGF-β plays a critical role in embryonic development, tissue homeostasis, and wound healing. It also has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

TGF-β exists in multiple isoforms (TGF-β1, TGF-β2, and TGF-β3) that are produced by many different cell types, including immune cells, epithelial cells, and fibroblasts. The protein is synthesized as a precursor molecule, which is cleaved to release the active TGF-β peptide. Once activated, TGF-β binds to its receptors on the cell surface, leading to the activation of intracellular signaling pathways that regulate gene expression and cell behavior.

In summary, Transforming Growth Factor-beta (TGF-β) is a multifunctional cytokine involved in various cellular processes, including cell growth, differentiation, apoptosis, embryonic development, tissue homeostasis, and wound healing. It has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

Sincalide is a synthetic hormone that stimulates the contraction of the gallbladder and the release of digestive enzymes from the pancreas. It is used in diagnostic procedures to help diagnose conditions such as gallstones or obstructions of the bile ducts.

Sincalide is a synthetic form of cholecystokinin (CCK), a hormone that is naturally produced in the body and stimulates the contraction of the gallbladder and the release of digestive enzymes from the pancreas. When sincalide is administered, it mimics the effects of CCK and causes the gallbladder to contract and release bile into the small intestine. This can help doctors see if there are any obstructions or abnormalities in the bile ducts or gallbladder.

Sincalide is usually given as an injection, and its effects can be monitored through imaging tests such as ultrasound or CT scans. It is important to note that sincalide should only be used under the supervision of a healthcare professional, as it can cause side effects such as abdominal pain, nausea, and vomiting.

Salivary alpha-amylases are a type of enzyme that are secreted by the salivary glands in humans and other mammals. These enzymes play a crucial role in the digestion of carbohydrates, specifically starches and glycogen, by breaking down these complex molecules into simpler sugars such as maltose, isomaltose, and maltotriose.

Salivary alpha-amylases are part of a larger family of enzymes known as alpha-amylases, which also include pancreatic alpha-amylases that are secreted by the pancreas and play a similar role in digestion. However, salivary alpha-amylases have some unique properties, such as being more resistant to denaturation by heat and acid than pancreatic alpha-amylases.

Salivary alpha-amylases are also used as a biomarker in forensic science for the identification of individuals, as they exhibit variations in their protein structure that can be used to distinguish between different people. Additionally, changes in salivary alpha-amylase levels have been associated with various physiological and psychological states, such as stress, anxiety, and arousal.

Trypsinogen is a precursor protein that is converted into the enzyme trypsin in the small intestine. It is produced by the pancreas and released into the duodenum, where it is activated by enterokinase, an enzyme produced by the intestinal mucosa. Trypsinogen plays a crucial role in digestion by helping to break down proteins into smaller peptides and individual amino acids.

In medical terms, an elevated level of trypsinogen in the blood may indicate pancreatic disease or injury, such as pancreatitis or pancreatic cancer. Therefore, measuring trypsinogen levels in the blood is sometimes used as a diagnostic tool to help identify these conditions.

Integrin α5β1, also known as very late antigen-5 (VLA-5) or fibronectin receptor, is a heterodimeric transmembrane receptor protein composed of two subunits: α5 and β1. This integrin is widely expressed in various cell types, including endothelial cells, smooth muscle cells, and fibroblasts.

Integrin α5β1 plays a crucial role in mediating cell-matrix adhesion by binding to the arginine-glycine-aspartic acid (RGD) sequence present in the extracellular matrix protein fibronectin. The interaction between integrin α5β1 and fibronectin is essential for various biological processes, such as cell migration, proliferation, differentiation, and survival. Additionally, this integrin has been implicated in several pathological conditions, including tumor progression, angiogenesis, and fibrosis.

Integrin beta4, also known as ITGB4 or CD104, is a type of integrin subunit that forms part of the integrin receptor along with an alpha subunit. Integrins are transmembrane proteins involved in cell-cell and cell-extracellular matrix (ECM) adhesion, signal transduction, and regulation of various cellular processes such as proliferation, differentiation, and migration.

Integrin beta4 is unique among the integrin subunits because it has a large cytoplasmic domain that can interact with several intracellular signaling molecules, making it an important regulator of cell behavior. Integrin beta4 is widely expressed in various tissues, including epithelial cells, endothelial cells, and hematopoietic cells.

Integrin beta4 forms heterodimers with integrin alpha6 to form the receptor for laminins, which are major components of the basement membrane. This receptor is involved in maintaining the integrity of epithelial tissues and regulating cell migration during development, tissue repair, and cancer progression. Mutations in ITGB4 have been associated with several human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and blistering.

Chymotrypsinogen is the inactive precursor form of the enzyme chymotrypsin, which is produced in the pancreas and plays a crucial role in digesting proteins in the small intestine. This zymogen is activated when it is cleaved by another protease called trypsin, resulting in the formation of the active enzyme chymotrypsin. Chymotrypsinogen is synthesized and stored in the pancreas as a proenzyme to prevent premature activation and potential damage to the pancreatic tissue. Once released into the small intestine, trypsin-mediated cleavage of chymotrypsinogen leads to the formation of chymotrypsin, which then contributes to protein breakdown and absorption in the gut.

Integrin α6β4 is a type of cell surface receptor that is composed of two subunits, α6 and β4. It is also known as CD49f/CD104. This integrin is primarily expressed in epithelial cells and plays important roles in cell adhesion, migration, and signal transduction.

Integrin α6β4 specifically binds to laminin-332 (also known as laminin-5), a component of the basement membrane, and forms a stable anchorage complex that links the cytoskeleton to the extracellular matrix. This interaction is critical for maintaining the integrity of epithelial tissues and regulating cell behavior during processes such as wound healing and tissue regeneration.

Mutations in the genes encoding integrin α6β4 have been associated with various human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and blistering. Additionally, integrin α6β4 has been implicated in cancer progression and metastasis, as its expression is often upregulated in tumor cells and contributes to their invasive behavior.

Integrin beta chains are a type of subunit that make up integrin receptors, which are heterodimeric transmembrane proteins involved in cell-cell and cell-extracellular matrix (ECM) adhesion. These receptors play crucial roles in various biological processes such as cell signaling, migration, proliferation, and differentiation.

Integrin beta chains combine with integrin alpha chains to form functional heterodimeric receptors. In humans, there are 18 different alpha subunits and 8 different beta subunits that can combine to form at least 24 distinct integrin receptors. The beta chain contributes to the cytoplasmic domain of the integrin receptor, which is involved in intracellular signaling and cytoskeletal interactions.

The beta chains are characterized by a conserved cytoplasmic region called the beta-tail domain, which interacts with various adaptor proteins to mediate downstream signaling events. Additionally, some integrin beta chains have a large inserted (I) domain in their extracellular regions that is responsible for ligand binding specificity.

Examples of integrin beta chains include β1, β2, β3, β4, β5, β6, β7, and β8, each with distinct functions and roles in various tissues and cell types. Mutations or dysregulation of integrin beta chains have been implicated in several human diseases, including cancer, inflammation, fibrosis, and developmental disorders.

Beta 2-glycoprotein I, also known as apolipoprotein H, is a plasma protein that belongs to the family of proteins called immunoglobulin-binding proteins. It has a molecular weight of approximately 44 kDa and is composed of five domains with similar structures.

Beta 2-glycoprotein I is primarily produced in the liver and circulates in the bloodstream, where it plays a role in several physiological processes, including coagulation, complement activation, and lipid metabolism. It has been identified as an autoantigen in certain autoimmune disorders, such as antiphospholipid syndrome (APS), where autoantibodies against beta 2-glycoprotein I can cause blood clots, miscarriages, and other complications.

In medical terminology, the definition of "beta 2-glycoprotein I" is as follows:

A plasma protein that belongs to the family of immunoglobulin-binding proteins and has a molecular weight of approximately 44 kDa. It is primarily produced in the liver and circulates in the bloodstream, where it plays a role in several physiological processes, including coagulation, complement activation, and lipid metabolism. Autoantibodies against beta 2-glycoprotein I are associated with certain autoimmune disorders, such as antiphospholipid syndrome (APS), where they can cause blood clots, miscarriages, and other complications.

Integrin α4β1, also known as Very Late Antigen-4 (VLA-4), is a heterodimeric transmembrane receptor protein composed of two subunits, α4 and β1. It is involved in various cellular activities such as adhesion, migration, and signaling. This integrin plays a crucial role in the immune system by mediating the interaction between leukocytes (white blood cells) and the endothelial cells that line blood vessels. The activation of Integrin α4β1 allows leukocytes to roll along and then firmly adhere to the endothelium, followed by their migration into surrounding tissues, particularly during inflammation and immune responses. Additionally, Integrin α4β1 also interacts with extracellular matrix proteins such as fibronectin and helps regulate cell survival, proliferation, and differentiation in various cell types.

Hyperamylasemia is a medical condition characterized by an elevated level of amylase in the blood. Amylase is an enzyme that is primarily produced by the pancreas and salivary glands, and it plays a crucial role in digesting carbohydrates.

Normally, the levels of amylase in the blood are relatively low, but when there is damage to the pancreas or salivary glands, such as in cases of pancreatitis, salivary gland inflammation, or blockage, the levels of amylase can rise significantly. This condition is called hyperamylasemia.

Mild elevations in amylase levels may not cause any symptoms and may be discovered only during routine blood tests. However, more significant elevations can indicate a serious underlying medical condition that requires prompt treatment. Symptoms of hyperamylasemia may include abdominal pain, nausea, vomiting, fever, and rapid heartbeat.

It is important to note that hyperamylasemia can also be caused by non-pancreatic conditions such as macroamylasemia, a benign condition where large amylase-containing protein complexes are formed and circulate in the bloodstream, leading to elevated amylase levels. Therefore, it is essential to perform further diagnostic tests to determine the underlying cause of hyperamylasemia.

The exocrine portion of the pancreas refers to the part that releases digestive enzymes into the duodenum, which is the first section of the small intestine. These enzymes help in the breakdown of proteins, fats, and carbohydrates in food, enabling their absorption and utilization by the body.

The exocrine pancreas is made up of acinar cells that cluster together to form acini (singular: acinus), which are small sac-like structures. When stimulated by hormones such as secretin and cholecystokinin, these acinar cells release digestive enzymes like amylase, lipase, and trypsin into a network of ducts that ultimately merge into the main pancreatic duct. This duct then joins the common bile duct, which carries bile from the liver and gallbladder, before emptying into the duodenum.

It is important to note that the pancreas has both exocrine and endocrine functions. The endocrine portion of the pancreas consists of the islets of Langerhans, which release hormones like insulin and glucagon directly into the bloodstream, regulating blood sugar levels.

Integrin α2β1, also known as very late antigen-2 (VLA-2) or laminin receptor, is a heterodimeric transmembrane receptor protein composed of α2 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α2β1 is widely expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some hematopoietic cells. It functions as a receptor for several ECM proteins, such as collagens (type I, II, III, and V), laminin, and fibronectin. The binding of integrin α2β1 to these ECM components mediates cell adhesion, migration, proliferation, differentiation, and survival, thereby regulating various physiological and pathological processes, such as tissue repair, angiogenesis, inflammation, and tumor progression.

In addition, integrin α2β1 has been implicated in several diseases, including fibrosis, atherosclerosis, and cancer. Therefore, targeting this integrin with therapeutic strategies may provide potential benefits for treating these conditions.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Beta-2 adrenergic receptors (β2-ARs) are a subtype of adrenergic receptors that are widely distributed throughout the body, particularly in the lungs, heart, blood vessels, gastrointestinal tract, and skeletal muscle.

When β2-ARs are activated by catecholamines, they trigger a range of physiological responses, including relaxation of smooth muscle, increased heart rate and contractility, bronchodilation, and inhibition of insulin secretion. These effects are mediated through the activation of intracellular signaling pathways involving G proteins and second messengers such as cyclic AMP (cAMP).

β2-ARs have been a major focus of drug development for various medical conditions, including asthma, chronic obstructive pulmonary disease (COPD), heart failure, hypertension, and anxiety disorders. Agonists of β2-ARs, such as albuterol and salmeterol, are commonly used to treat asthma and COPD by relaxing bronchial smooth muscle and reducing airway obstruction. Antagonists of β2-ARs, such as propranolol, are used to treat hypertension, angina, and heart failure by blocking the effects of catecholamines on the heart and blood vessels.

Bethanechol compounds are a type of cholinergic agent used in medical treatment. They are parasympathomimetic drugs, which means they mimic the actions of the neurotransmitter acetylcholine at muscarinic receptors. Specifically, bethanechol compounds stimulate the muscarinic receptors in the smooth muscle of the bladder and gastrointestinal tract, increasing tone and promoting contractions.

Bethanechol is primarily used to treat urinary retention and associated symptoms, such as those that can occur after certain types of surgery or with conditions like spinal cord injury or multiple sclerosis. It works by helping the bladder muscle contract, which can promote urination.

It's important to note that bethanechol should be used with caution, as it can have various side effects, including sweating, increased salivation, flushed skin, and gastrointestinal symptoms like nausea, vomiting, or diarrhea. It may also interact with other medications, so it's crucial to discuss any potential risks with a healthcare provider before starting this treatment.

Salivary proteins and peptides refer to the diverse group of molecules that are present in saliva, which is the clear, slightly alkaline fluid produced by the salivary glands in the mouth. These proteins and peptides play a crucial role in maintaining oral health and contributing to various physiological functions.

Some common types of salivary proteins and peptides include:

1. **Mucins**: These are large, heavily glycosylated proteins that give saliva its viscous quality. They help to lubricate the oral cavity, protect the mucosal surfaces, and aid in food bolus formation.
2. **Amylases**: These enzymes break down carbohydrates into simpler sugars, initiating the digestive process even before food reaches the stomach.
3. **Proline-rich proteins (PRPs)**: PRPs contribute to the buffering capacity of saliva and help protect against tooth erosion by forming a protective layer on tooth enamel.
4. **Histatins**: These are small cationic peptides with antimicrobial properties, playing a significant role in maintaining oral microbial homeostasis and preventing dental caries.
5. **Lactoferrin**: An iron-binding protein that exhibits antibacterial, antifungal, and anti-inflammatory activities, contributing to the overall oral health.
6. **Statherin and Cystatins**: These proteins regulate calcium phosphate precipitation, preventing dental calculus formation and maintaining tooth mineral homeostasis.

Salivary proteins and peptides have attracted significant interest in recent years due to their potential diagnostic and therapeutic applications. Alterations in the composition of these molecules can provide valuable insights into various oral and systemic diseases, making them promising biomarkers for disease detection and monitoring.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Secretory rate refers to the amount or volume of a secretion produced by a gland or an organ over a given period of time. It is a measure of the productivity or activity level of the secreting structure. The secretory rate can be quantified for various bodily fluids, such as saliva, sweat, digestive enzymes, hormones, or milk, depending on the context and the specific gland or organ being studied.

In clinical settings, measuring the secretory rate might involve collecting and analyzing samples over a certain duration to estimate the production rate of the substance in question. This information can be helpful in diagnosing conditions related to impaired secretion, monitoring treatment responses, or understanding the physiological adaptations of the body under different circumstances.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.

Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).

These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.

Interleukin-1 (IL-1) is a type of cytokine, which are proteins that play a crucial role in cell signaling. Specifically, IL-1 is a pro-inflammatory cytokine that is involved in the regulation of immune and inflammatory responses in the body. It is produced by various cells, including monocytes, macrophages, and dendritic cells, in response to infection or injury.

IL-1 exists in two forms, IL-1α and IL-1β, which have similar biological activities but are encoded by different genes. Both forms of IL-1 bind to the same receptor, IL-1R, and activate intracellular signaling pathways that lead to the production of other cytokines, chemokines, and inflammatory mediators.

IL-1 has a wide range of biological effects, including fever induction, activation of immune cells, regulation of hematopoiesis (the formation of blood cells), and modulation of bone metabolism. Dysregulation of IL-1 production or activity has been implicated in various inflammatory diseases, such as rheumatoid arthritis, gout, and inflammatory bowel disease. Therefore, IL-1 is an important target for the development of therapies aimed at modulating the immune response and reducing inflammation.

CD29, also known as integrin β1, is a type of cell surface protein called an integrin that forms heterodimers with various α subunits to form different integrin receptors. These integrin receptors play important roles in various biological processes such as cell adhesion, migration, and signaling.

CD29/integrin β1 is widely expressed on many types of cells including leukocytes, endothelial cells, epithelial cells, and fibroblasts. It can bind to several extracellular matrix proteins such as collagen, laminin, and fibronectin, and mediate cell-matrix interactions. CD29/integrin β1 also participates in intracellular signaling pathways that regulate cell survival, proliferation, differentiation, and migration.

CD29/integrin β1 can function as an antigen, which is a molecule capable of inducing an immune response. Antibodies against CD29/integrin β1 have been found in some autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus (SLE). These antibodies can contribute to the pathogenesis of these diseases by activating complement, inducing inflammation, and damaging tissues.

Therefore, CD29/integrin β1 is an important molecule in both physiological and pathological processes, and its functions as an antigen have been implicated in some autoimmune disorders.

Integrin α6β1, also known as CD49f/CD29, is a heterodimeric transmembrane receptor protein composed of α6 and β1 subunits. It is widely expressed in various tissues, including epithelial cells, endothelial cells, fibroblasts, and hematopoietic cells. Integrin α6β1 plays a crucial role in cell-matrix adhesion, particularly to the laminin component of the extracellular matrix (ECM). This receptor is involved in various biological processes such as cell migration, proliferation, differentiation, and survival. Additionally, integrin α6β1 has been implicated in tumor progression, metastasis, and drug resistance in certain cancers.

Isoproterenol is a medication that belongs to a class of drugs called beta-adrenergic agonists. Medically, it is defined as a synthetic catecholamine with both alpha and beta adrenergic receptor stimulating properties. It is primarily used as a bronchodilator to treat conditions such as asthma and chronic obstructive pulmonary disease (COPD) by relaxing the smooth muscles in the airways, thereby improving breathing.

Isoproterenol can also be used in the treatment of bradycardia (abnormally slow heart rate), cardiac arrest, and heart blocks by increasing the heart rate and contractility. However, due to its non-selective beta-agonist activity, it may cause various side effects such as tremors, palpitations, and increased blood pressure. Its use is now limited due to the availability of more selective and safer medications.

An acute disease is a medical condition that has a rapid onset, develops quickly, and tends to be short in duration. Acute diseases can range from minor illnesses such as a common cold or flu, to more severe conditions such as pneumonia, meningitis, or a heart attack. These types of diseases often have clear symptoms that are easy to identify, and they may require immediate medical attention or treatment.

Acute diseases are typically caused by an external agent or factor, such as a bacterial or viral infection, a toxin, or an injury. They can also be the result of a sudden worsening of an existing chronic condition. In general, acute diseases are distinct from chronic diseases, which are long-term medical conditions that develop slowly over time and may require ongoing management and treatment.

Examples of acute diseases include:

* Acute bronchitis: a sudden inflammation of the airways in the lungs, often caused by a viral infection.
* Appendicitis: an inflammation of the appendix that can cause severe pain and requires surgical removal.
* Gastroenteritis: an inflammation of the stomach and intestines, often caused by a viral or bacterial infection.
* Migraine headaches: intense headaches that can last for hours or days, and are often accompanied by nausea, vomiting, and sensitivity to light and sound.
* Myocardial infarction (heart attack): a sudden blockage of blood flow to the heart muscle, often caused by a buildup of plaque in the coronary arteries.
* Pneumonia: an infection of the lungs that can cause coughing, chest pain, and difficulty breathing.
* Sinusitis: an inflammation of the sinuses, often caused by a viral or bacterial infection.

It's important to note that while some acute diseases may resolve on their own with rest and supportive care, others may require medical intervention or treatment to prevent complications and promote recovery. If you are experiencing symptoms of an acute disease, it is always best to seek medical attention to ensure proper diagnosis and treatment.

Adrenergic beta-agonists are a class of medications that bind to and activate beta-adrenergic receptors, which are found in various tissues throughout the body. These receptors are part of the sympathetic nervous system and mediate the effects of the neurotransmitter norepinephrine (also called noradrenaline) and the hormone epinephrine (also called adrenaline).

When beta-agonists bind to these receptors, they stimulate a range of physiological responses, including relaxation of smooth muscle in the airways, increased heart rate and contractility, and increased metabolic rate. As a result, adrenergic beta-agonists are often used to treat conditions such as asthma, chronic obstructive pulmonary disease (COPD), and bronchitis, as they can help to dilate the airways and improve breathing.

There are several different types of beta-agonists, including short-acting and long-acting formulations. Short-acting beta-agonists (SABAs) are typically used for quick relief of symptoms, while long-acting beta-agonists (LABAs) are used for more sustained symptom control. Examples of adrenergic beta-agonists include albuterol (also known as salbutamol), terbutaline, formoterol, and salmeterol.

It's worth noting that while adrenergic beta-agonists can be very effective in treating respiratory conditions, they can also have side effects, particularly if used in high doses or for prolonged periods of time. These may include tremors, anxiety, palpitations, and increased blood pressure. As with any medication, it's important to use adrenergic beta-agonists only as directed by a healthcare professional.

Beta-1 adrenergic receptors (also known as β1-adrenergic receptors) are a type of G protein-coupled receptor found in the cell membrane. They are activated by the catecholamines, particularly noradrenaline (norepinephrine) and adrenaline (epinephrine), which are released by the sympathetic nervous system as part of the "fight or flight" response.

When a catecholamine binds to a β1-adrenergic receptor, it triggers a series of intracellular signaling events that ultimately lead to an increase in the rate and force of heart contractions, as well as an increase in renin secretion from the kidneys. These effects help to prepare the body for physical activity by increasing blood flow to the muscles and improving the efficiency of the cardiovascular system.

In addition to their role in the regulation of cardiovascular function, β1-adrenergic receptors have been implicated in a variety of physiological processes, including lipolysis (the breakdown of fat), glucose metabolism, and the regulation of mood and cognition.

Dysregulation of β1-adrenergic receptor signaling has been linked to several pathological conditions, including heart failure, hypertension, and anxiety disorders. As a result, β1-adrenergic receptors are an important target for the development of therapeutics used in the treatment of these conditions.

Secretin is a hormone that is produced and released by the S cells in the duodenum, which is the first part of the small intestine. It is released in response to the presence of acidic chyme (partially digested food) entering the duodenum from the stomach. Secretin stimulates the pancreas to produce bicarbonate-rich alkaline secretions, which help neutralize the acidity of the chyme and create an optimal environment for enzymatic digestion in the small intestine.

Additionally, secretin also promotes the production of watery fluids from the liver, which aids in the digestion process. Overall, secretin plays a crucial role in maintaining the pH balance and facilitating proper nutrient absorption in the gastrointestinal tract.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Maltose is a disaccharide made up of two glucose molecules joined by an alpha-1,4 glycosidic bond. It is commonly found in malted barley and is created during the germination process when amylase breaks down starches into simpler sugars. Maltose is less sweet than sucrose (table sugar) and is broken down into glucose by the enzyme maltase during digestion.

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.

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.

Integrin α1β1, also known as Very Late Antigen-1 (VLA-1) or CD49a/CD29, is a heterodimeric transmembrane receptor protein composed of α1 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α1β1 is primarily expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some immune cells. This integrin binds to several ECM proteins, such as collagens (type I, II, III, IV), laminin, and fibronectin, mediating cell adhesion, migration, proliferation, differentiation, and survival. Additionally, α1β1 integrin has been implicated in various physiological and pathological processes, such as tissue repair, fibrosis, and tumor progression.

Pancreatic diseases refer to a group of medical conditions that affect the structure and function of the pancreas, a vital organ located in the abdomen. The pancreas has two main functions: an exocrine function, which involves the production of digestive enzymes that help break down food in the small intestine, and an endocrine function, which involves the production of hormones such as insulin and glucagon that regulate blood sugar levels.

Pancreatic diseases can be broadly classified into two categories: inflammatory and non-inflammatory. Inflammatory pancreatic diseases include conditions such as acute pancreatitis, which is characterized by sudden inflammation of the pancreas, and chronic pancreatitis, which is a long-term inflammation that can lead to scarring and loss of function.

Non-inflammatory pancreatic diseases include conditions such as pancreatic cancer, which is a malignant tumor that can arise from the cells of the pancreas, and benign tumors such as cysts or adenomas. Other non-inflammatory conditions include pancreatic insufficiency, which can occur when the pancreas does not produce enough digestive enzymes, and diabetes mellitus, which can result from impaired insulin production or action.

Overall, pancreatic diseases can have serious consequences on a person's health and quality of life, and early diagnosis and treatment are essential for optimal outcomes.

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.

Glycogen Synthase Kinase 3 (GSK-3) is a serine/threonine protein kinase that plays a crucial role in the regulation of several cellular processes, including glycogen metabolism, cell signaling, gene transcription, and apoptosis. It was initially discovered as a key enzyme involved in glycogen metabolism due to its ability to phosphorylate and inhibit glycogen synthase, an enzyme responsible for the synthesis of glycogen from glucose.

GSK-3 exists in two isoforms, GSK-3α and GSK-3β, which share a high degree of sequence similarity and are widely expressed in various tissues. Both isoforms are constitutively active under normal conditions and are regulated through inhibitory phosphorylation by several upstream signaling pathways, such as insulin, Wnt, and Hedgehog signaling.

Dysregulation of GSK-3 has been implicated in the pathogenesis of various diseases, including diabetes, neurodegenerative disorders, and cancer. In recent years, GSK-3 has emerged as an attractive therapeutic target for the development of novel drugs to treat these conditions.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Estrogen Receptor beta (ER-β) is a protein that is encoded by the gene ESR2 in humans. It belongs to the family of nuclear receptors, which are transcription factors that regulate gene expression in response to hormonal signals. ER-β is one of two main estrogen receptors, the other being Estrogen Receptor alpha (ER-α), and it plays an important role in mediating the effects of estrogens in various tissues, including the breast, uterus, bone, brain, and cardiovascular system.

Estrogens are steroid hormones that play a critical role in the development and maintenance of female reproductive and sexual function. They also have important functions in other tissues, such as maintaining bone density and promoting cognitive function. ER-β is widely expressed in many tissues, including those outside of the reproductive system, suggesting that it may have diverse physiological roles beyond estrogen-mediated reproduction.

ER-β has been shown to have both overlapping and distinct functions from ER-α, and its expression patterns differ between tissues. For example, in the breast, ER-β is expressed at higher levels in normal tissue compared to cancerous tissue, suggesting that it may play a protective role against breast cancer development. In contrast, in the uterus, ER-β has been shown to have anti-proliferative effects and may protect against endometrial cancer.

Overall, ER-β is an important mediator of estrogen signaling and has diverse physiological roles in various tissues. Understanding its functions and regulation may provide insights into the development of novel therapies for a range of diseases, including cancer, osteoporosis, and cardiovascular disease.

Clinical enzyme tests are laboratory tests that measure the amount or activity of certain enzymes in biological samples, such as blood or bodily fluids. These tests are used to help diagnose and monitor various medical conditions, including organ damage, infection, inflammation, and genetic disorders.

Enzymes are proteins that catalyze chemical reactions in the body. Some enzymes are found primarily within specific organs or tissues, so elevated levels of these enzymes in the blood can indicate damage to those organs or tissues. For example, high levels of creatine kinase (CK) may suggest muscle damage, while increased levels of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) can indicate liver damage.

There are several types of clinical enzyme tests, including:

1. Serum enzyme tests: These measure the level of enzymes in the blood serum, which is the liquid portion of the blood after clotting. Examples include CK, AST, ALT, alkaline phosphatase (ALP), and lactate dehydrogenase (LDH).
2. Urine enzyme tests: These measure the level of enzymes in the urine. An example is N-acetyl-β-D-glucosaminidase (NAG), which can indicate kidney damage.
3. Enzyme immunoassays (EIAs): These use antibodies to detect and quantify specific enzymes or proteins in a sample. They are often used for the diagnosis of infectious diseases, such as HIV or hepatitis.
4. Genetic enzyme tests: These can identify genetic mutations that cause deficiencies in specific enzymes, leading to inherited metabolic disorders like phenylketonuria (PKU) or Gaucher's disease.

It is important to note that the interpretation of clinical enzyme test results should be done by a healthcare professional, taking into account the patient's medical history, symptoms, and other diagnostic tests.

Pancreatic alpha-amylases are a type of enzyme that is produced and secreted by the exocrine cells (acinar cells) of the pancreas. These enzymes play an essential role in digesting carbohydrates, particularly starches and glycogen, which are complex forms of carbohydrates found in various foods like grains, potatoes, and legumes.

Alpha-amylases break down these complex carbohydrates into smaller, simpler sugars, such as maltose, maltotriose, and glucose, allowing for their absorption and utilization by the body. The pancreatic alpha-amylases are released into the duodenum, the first part of the small intestine, along with other digestive enzymes during the process of digestion.

In addition to pancreatic alpha-amylases, salivary glands also produce a form of amylase called salivary alpha-amylase, which initiates the breakdown of starches in the mouth through mastication (chewing). However, the majority of carbohydrate digestion occurs in the small intestine with the help of pancreatic alpha-amylases and other enzymes produced by the intestinal lining.

Transforming Growth Factor-beta 1 (TGF-β1) is a cytokine that belongs to the TGF-β superfamily. It is a multifunctional protein involved in various cellular processes, including cell growth, differentiation, apoptosis, and extracellular matrix production. TGF-β1 plays crucial roles in embryonic development, tissue homeostasis, and repair, as well as in pathological conditions such as fibrosis and cancer. It signals through a heteromeric complex of type I and type II serine/threonine kinase receptors, leading to the activation of intracellular signaling pathways, primarily the Smad-dependent pathway. TGF-β1 has context-dependent functions, acting as a tumor suppressor in normal and early-stage cancer cells but promoting tumor progression and metastasis in advanced cancers.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Carbachol is a cholinergic agonist, which means it stimulates the parasympathetic nervous system by mimicking the action of acetylcholine, a neurotransmitter that is involved in transmitting signals between nerves and muscles. Carbachol binds to both muscarinic and nicotinic receptors, but its effects are more pronounced on muscarinic receptors.

Carbachol is used in medical treatments to produce miosis (pupil constriction), lower intraocular pressure, and stimulate gastrointestinal motility. It can also be used as a diagnostic tool to test for certain conditions such as Hirschsprung's disease.

Like any medication, carbachol can have side effects, including sweating, salivation, nausea, vomiting, diarrhea, bradycardia (slow heart rate), and bronchoconstriction (narrowing of the airways in the lungs). It should be used with caution and under the supervision of a healthcare professional.

Beta-3 adrenergic receptors (β3-AR) are a type of G protein-coupled receptor that binds catecholamines, such as norepinephrine and epinephrine. These receptors are primarily located in the adipose tissue, where they play a role in regulating lipolysis (the breakdown of fat) and thermogenesis (the production of heat).

Activation of β3-AR stimulates the enzyme hormone-sensitive lipase, which leads to the hydrolysis of triglycerides and the release of free fatty acids. This process is important for maintaining energy homeostasis and can be activated through exercise, cold exposure, or pharmacological means.

In addition to their role in metabolism, β3-AR have also been implicated in the regulation of cardiovascular function, bladder function, and inflammation. Selective β3-AR agonists are being investigated as potential therapeutic agents for the treatment of obesity, type 2 diabetes, and nonalcoholic fatty liver disease.

A dose-response relationship in the context of drugs refers to the changes in the effects or symptoms that occur as the dose of a drug is increased or decreased. Generally, as the dose of a drug is increased, the severity or intensity of its effects also increases. Conversely, as the dose is decreased, the effects of the drug become less severe or may disappear altogether.

The dose-response relationship is an important concept in pharmacology and toxicology because it helps to establish the safe and effective dosage range for a drug. By understanding how changes in the dose of a drug affect its therapeutic and adverse effects, healthcare providers can optimize treatment plans for their patients while minimizing the risk of harm.

The dose-response relationship is typically depicted as a curve that shows the relationship between the dose of a drug and its effect. The shape of the curve may vary depending on the drug and the specific effect being measured. Some drugs may have a steep dose-response curve, meaning that small changes in the dose can result in large differences in the effect. Other drugs may have a more gradual dose-response curve, where larger changes in the dose are needed to produce significant effects.

In addition to helping establish safe and effective dosages, the dose-response relationship is also used to evaluate the potential therapeutic benefits and risks of new drugs during clinical trials. By systematically testing different doses of a drug in controlled studies, researchers can identify the optimal dosage range for the drug and assess its safety and efficacy.

"Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. Beta-amylase at the U.S. National Library of Medicine Medical ... The optimum pH for β-amylase is 4.0-5.0 They belong to Glycoside hydrolase family 14. Amylase Alpha-amylase Rejzek M, Stevenson ... glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. Beta-amylase is found in ... β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It ...
Beta-amylase is present in certain bacteria as well as in plants. Three highly conserved sequence regions are found in all ... while the smaller is formed from two long loops extending from the beta-3 and beta-4 strands of the (beta alpha)8 fold. The ... Beta-amylase is an enzyme that hydrolyzes 1,4-alpha-glucosidic linkages in starch-type polysaccharide substrates so as to ... The 3D structure of a complex of soybean beta-amylase with an inhibitor (alpha-cyclodextrin) has been determined to 3.0A ...
Oyama, T.; Kusunoki, M.; Kishimoto, Y.; Takasaki, Y.; Nitta, Y. (1999). "Crystal structure of beta-amylase from Bacillus cereus ... It has a beta-jelly roll fold, with a groove on the concave surface of one of the beta-sheets. Carbohydrate-binding module ... CBM27 adopts a beta sandwich structure comprising 13 beta strands with a single, small alpha-helix and a single metal atom. ... It has a budded fibronectin type III fold consisting of two beta-sheets, arranged as a beta-sheet sandwich and a bud consisting ...
Different temperatures optimize the activity of alpha or beta amylase, resulting in different mixtures of fermentable and ... Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α- ... In human physiology, both the salivary and pancreatic amylases are α-amylases. The α-amylase form is also found in plants, ... The γ-amylase has the most acidic optimum pH of all amylases because it is most active around pH 3. They belong to a variety of ...
MacGregor EA, Jespersen HM, Svensson B (January 1996). "A circularly permuted alpha-amylase-type alpha/beta-barrel structure in ... have a different arrangement than those in α-amylase. The folding characteristics of α-amylase and glucansucrase are still very ... However, glucansucrase is very similar to α-amylase, another sugar-cutting enzyme. Glucansucrase thus has many of the same ... Glucansucrase proteins likely evolved from an amylase enzyme precursor. The two enzymes have similar folding patterns and ...
When beta-amylase breaks down starch, it removes two glucose units at a time, producing maltose. An example of this reaction is ...
These test include: catalase, urease, oxidase, amylase, gelatins, phosphatase, beta-galactosidase activities, and carbon source ...
For spinach leaves, Alpha-amylase is preferred but for plants/organisms like wheat, barley, peas, etc. the Beta-amylase is ... in which the chloroplast contains both alpha and beta amylase (They are different versions of amylase involved in the breakdown ... The difference between chloroplast and extrachloroplastic starch degradation is in the amylase pathway they prefer; either beta ... Turning starch into sugar is done by the enzyme amylase. The process in which amylase breaks down starch for sugar consumption ...
After the phosphorylation, the first degrading enzyme, beta-amylase (BAM) can attack the glucose chain at its non-reducing end ... This is in contrast to many structural polysaccharides such as chitin, cellulose and peptidoglycan, which are bound by beta ... In this cell-free biosystem, beta-1,4-glycosidic bond-linked cellulose is partially hydrolyzed to cellobiose. Cellobiose ...
Unconverted starch becomes sugar during the last steps of mashing, through the action of alpha and beta amylases. The oldest ... Germination produces a number of enzymes, such as amylase, that can convert the starch naturally present in barley and other ... thorough beta-glucanase rest. Rye is said to impart a spicy, dry flavor to beer. Sorghum and millet are often used in African ... and contains large quantities of beta-glucans compared to other grains; these long-chain sugars can leach out during a mash, ...
Beta) Limit dextrin is the remaining polymer produced by enzymatic hydrolysis of amylopectin with beta amylase, which cannot ... Dextrins can be produced from starch using enzymes like amylases, as during digestion in the human body and during malting and ... produced by hydrolysis of amylopectin with alpha amylase. Highly branched cyclic dextrin is a dextrin produced from enzymatic ...
The enzymes used in the saccharification step are the amylolytic enzyme, beta-amylase (usually derived from Bacillus species) ... Such syrups are high in the simple sugar maltose and low in glucose and fructose, due to the enzymatic action of beta- and ... The enzymes used in the liquefaction step are usually alpha-amylases derived from bacterial or fungal bioreactors (Bacillus ... alpha amylase on starch supplied by the sprouted barley. These enzymes produce large amounts of maltose from starch digestion ...
To overcome this, producers use an enzymatic hydrolysis of starch by alpha- and beta-amylase, which break down the starch into ...
... alpha and beta amylase, and, to a lesser extent, gamma amylase (together, the amylases), although many other enzymes are also ... Today, "diastase" refers to any α-, β-, or γ-amylase (all of which are hydrolases) that can break down carbohydrates. The ... When used as a pharmaceutical drug, diastase has the ATC code A09AA01 (WHO). Amylases can also be extracted from other sources ... Takadiastase Whipple disease Amylase Gray, G.M. (1975). "Carbohydrate digestion and absorption". New England Journal of ...
... that recognizes SP8 sequences in the 50 upstream regions of genes coding for sporamin and beta-amylase from sweet potato. Mol. ... The earliest reports identified WRKYs based on their ability to regulate β-amylase, a gene involved in catabolism of starch ... upstream regions of genes coding for sporamin and β-amylase from sweet potato. Molecular and General Genetics. 244(6). 563-571 ... upstream regions of genes coding for sporamin and β-amylase from sweet potato. Molecular and General Genetics. 244(6). 563-571 ...
... elegans produces amylase, beta-glucosidase, cellulase, and protease. It is able to degrade cellulose. When M. elegans is grown ...
... alpha-amylase, pullulanase, beta-amylase, and alpha-D-glucosidase) and only achieves a 40% yield of isomaltooligosaccharides ... also known as an alpha/beta barrel), an alpha/beta protein fold structure consisting of eight parallel beta-strands connected ... While most alpha-amylase enzymes only cleave alpha-1,4-linkages in their substrates, neopullulanase additionally cleaves alpha- ... This results in narrower active site than the other alpha-amylase enzymes, which do not dimerize, and likely contributes to its ...
Organisms meant to produce enzymes such as beta galactosidase, invertase or other amylases may be fed starch to select for ... Of primary interest among the intracellular components are microbial enzymes: catalase, amylase, protease, pectinase, cellulase ...
Research Service scientists are interested in specialized enzymes called serine-class proteases that digest beta-amylases, ... Malted grain that has been ground into a coarse meal is known as "sweet meal". Malting grain develops the enzymes (α-amylase, β ... amylase) required for modifying the grains' starches into various types of sugar, including monosaccharide glucose, ... that has undergone preparation to activate the natural amylase and glucanase enzymes in the grain. Initially researched as an ...
The breakdown of starch is dependent on three enzymes, among others: alpha, beta amylases phosphorylases starch debranching ... Humans and other animals that eat plant foods also use amylase, an enzyme that assists in breaking down amylopectin, to ... degraded by b-amylase only to the stage of residual dextrin". Meyer also proposed the tree like structure model for amylopectin ...
Glucose Amylase/lipase Urine culture Urinalysis Beta-human chorionic gonadotropin (beta-hCG) Cervical cultures are recommended ...
... they are connected via an alpha 1-4 linkage instead of beta. Starches, particularly amylase, are important in many industries, ... There are also conformations that consist of a mix of alpha helices and beta sheets as well as a beta helixes with an alpha ... Beta is a protein that binds to single stranded DNA and assists homologous recombination by promoting annealing between the ... Cellulose is a polysaccharide made up of beta 1-4 linkages between repeat glucose monomers. It is the most abundant source of ...
... amylases MeSH D08.811.277.450.066.050 - alpha-amylase MeSH D08.811.277.450.066.100 - beta-amylase MeSH D08.811.277.450.114 - ... 4-beta-glucosidase MeSH D08.811.277.450.420.200.600 - glucan endo-1,3-beta-d-glucosidase MeSH D08.811.277.450.420.375 - glucan ... 4-beta-cellobiosidase MeSH D08.811.277.450.420.200.450 - endo-1,3(4)-beta-glucanase MeSH D08.811.277.450.420.200.500 - glucan 1 ... 4-beta xylanases MeSH D08.811.277.450.950.500 - xylan endo-1,3-beta-xylosidase MeSH D08.811.277.656.149 - atp-dependent ...
It has been shown that more than 600 proteins with various function (e.g., oxidase, dismutase, amylase) contain the beta barrel ... Explanation of all-beta topologies: "orthogonal beta-sandwiches" are beta-barrels (as defined in this article); "aligned" beta- ... Beta-strands in many beta-barrels are arranged in an antiparallel fashion. Beta barrel structures are named for resemblance to ... Likewise, a beta barrel can be formed by bringing the edges of a beta sheet together to form a cylinder. If those edges are ...
... which is then removed by hydrolysis with alpha-amylase. The residual solution usually contains coextracts of hemicelluloses and ... 1160/2011 of the Commission, foodstuffs through which 3 g/day of oat beta-glucan are consumed (1 g of oat beta-glucan per ... In November 2011, the EU Commission published its decision in favour of oat beta-glucans with regard to Article 14 of the EC ... Diabetic people who increased their daily consumption of beta-glucans by more than 3 grams per day for months also lost body ...
Organisms can either by alpha-hemolytic, beta-hemolytic, or gamma-hemolytic (non-hemolytic). Amylases are a group of ... The different classes of amylases are α-amylases, β-amylases, and glucoamylases. The α-amylases hydrolyze starch by randomly ... Amylase breaks down carbohydrates into mono- and disaccharides, so a starch agar must be used for this assay. Once the bacteria ... In humans, amylases are secreted by the pancreas and salivary glands, with both sources of the enzyme required for complete ...
... the soluble fraction of alpha-amylase hydrolyzed oat bran or whole oat flour), whole grain barley and barley beta-fiber. An ... Beta-glucans, β-glucans comprise a group of β-D-glucose polysaccharides (glucans) naturally occurring in the cell walls of ... Each type of beta-glucan comprises a different molecular backbone, level of branching, and molecular weight which affects its ... beta-Glucans at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short description, Short ...
... beta-cyclodextrin glucanotransferase, beta-cyclodextrin glycosyltransferase, gamma-cyclodextrin glycosyltransferase, ... They are bacterial enzymes belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13. ... Co-substrate specificity in coupling reactions of Macerans amylase". J. Am. Chem. Soc. 76 (9): 2387-2390. doi:10.1021/ ... DePinto JA, Campbell LL (1968). "Purification and properties of the amylase of Bacillus macerans". Biochemistry. 7 (1): 114-20 ...
Beta-galactosidase (EC 3.2.1.23) Hyaluronidase (EC 3.2.1.35) Function: Amylase is an enzyme that is responsible for the ... Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the ... EC 3.2.1 Amylase (EC 3.2.1.1) Sucrase (EC 3.2.1.10) Chitinase (EC 3.2.1.14) Lysozyme (EC 3.2.1.17) Maltase (EC 3.2.1.20) ... Beta-lactamase (EC 3.5.2.6) Category:EC 3.5.3 (In linear amidines) Arginase (EC 3.5.3.1) Category:EC 3.5.4 (In cyclic amidines ...
Malt made from barley is used as a source of β-amylase to break down starch into the disaccharide maltose, which can be used by ... Cellulose is first hydrolyzed to cellobiose by cellulase and then cellobiose is further hydrolyzed to glucose by beta- ... Other amylase enzymes may convert starch to glucose or to oligosaccharides. ...
Recombinant Arabidopsis thaliana Beta-amylase 1, chloroplastic (BAM1) , partial from Cusabio. Cat Number: CSB-YP878501DOA. USA ... Alternative Name(s): 1,4-alpha-D-glucan maltohydrolase () () () () () () () Beta-amylase 7 Thioredoxin-regulated beta-amylase ... Recombinant Arabidopsis thaliana Beta-amylase 1, chloroplastic (BAM1) , partial , CSB-YP878501DOA. (No reviews yet) Write a ... Recombinant Arabidopsis thaliana Beta-amylase 1, chloroplastic (BAM1) , partial , CSB-YP878501DOA Cusabio Arabidopsis thaliana ...
... in the largest biology dictionary online. Free learning resources for students covering all major areas of biology ... Beta-amylase. Definition noun, plural: beta-amylases A form of amylase found in bacteria, molds, yeasts, and the seeds of ... noun, plural: beta-amylases. A form of amylase found in bacteria, molds, yeasts, and the seeds of plants that cuts alpha-bonds ... removing the successive beta-maltose units from the non-reducing ends of the chains. Supplement In plants, the β-amylase breaks ...
Buy alpha and beta amylase online from China. ... Good quality alpha and beta amylase from alpha and beta amylase ... Beige Yellow Alpha Amylase Enzyme Powder , Heat - Stable Enzyme Alpha Amylase. * High Concentration Alpha Amylase Enzyme 40000 ... Food Grade Alpha And Beta Amylase , Bacterial Starch Digesting Enzyme PH 5.8 To 6.8. Get Best Price ... Commercial Alpha Amylase Brewing , Food Grade Low PH Fungal Amylase Enzymes For Starch Sugar. Get Best Price ...
beta-amylase; 4-alpha-D-glucan maltohydrolase Source. Hordeum Vulgare Molecular Weight. 58300 ... β-Amylase (Barley) - English - Ireland β-Amylase (Barley) - English - New Zealand β-Amylase (Barley) - English - US β-Amylase ( ... β-Amylase (Barley) - French β-Amylase (Barley) - German β-Amylase (Barley) - Greek - Greece β-Amylase (Barley) - Hungarian - ... β-Amylase (Barley) - Italian - Italy β-Amylase (Barley) - Japanese - Japan β-Amylase (Barley) - Latvian - Latvia β-Amylase ( ...
Crystal Structure of a Beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltose ... Crystal Structure of a Beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltose Coordinates. PDB Format ... Miyake, H. et al., Crystal Structure of a Catalytic Site Mutant of beta-Amylase from Bacillus cereus var. mycoides ... 2 x BGC- GLC: alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose(Non-covalent). BGC-GLC.2: 14 residues within 4Å:*. Chain A: W. ...
"Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase. Beta-amylase at the U.S. National Library of Medicine Medical ... The optimum pH for β-amylase is 4.0-5.0 They belong to Glycoside hydrolase family 14. Amylase Alpha-amylase Rejzek M, Stevenson ... glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. Beta-amylase is found in ... β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It ...
You are using . If you find that the function is abnormal, please change your browser and try again.. It is highly recommended that you use a faster and more secure Google Chrome. ...
Amylase (Diastase) is one of the subject in which we provide homework and Assignment Help. Our feature includes 24x7 live ... Amylase is divided in three types : a) Alpha-amylase, b) Beta-amylase, and c) Gamma-amylase. These types are differentiate on ... Amylase (Diastase) Project Help , Help For Amylase (Diastase) , Help Amylase (Diastase), Help On Amylase (Diastase) , Amylase ( ... To submit Amylase (Diastase) assignment click here.. Amylase (Diastase) Help , Amylase (Diastase) Homework Help ,Amylase ( ...
Shop online from a wide range of beta glucanase. ... Beta Glucanase. Who are the top beta glucanase manufacturers in ... Find beta glucanase manufacturers, suppliers, dealers & latest prices from top companies in India. ... Beta Glucanase. Wood Preservative. Calcined Magnesium Oxide. Zinc Phosphate. Lithium Nitride. Red Mercuric Oxide. Per Chloro ... How many trusted sellers are available for beta glucanase?. +. There are six trusted sellers of beta glucanase, and their names ...
... maltose of Bacillus cereus Beta-Amylase at pH 6.5. Class: hydrolase. Keywords: beta-alpha-barrels, optimum pH, T47M/Y164E/T328N ... Compound: beta-amylase. Species: Bacillus cereus [TaxId:1396]. Database cross-references and differences (RAF-indexed): * ...
Bernfeld, P. (1955). Amylases, alpha and beta. Methods Enzymol. 1, 149-154. ... One unit of amylase activity was defined as the amount of enzyme needed to catalyze the production of 1 μg of p-nitrophenol per ... One unit of amylase activity was defined as the amount of enzyme needed to catalyze the formation of 1 μg of maltose equivalent ... Figure 3. Beta diversity and alpha diversity of gut microbiota of gilthead sea bream fed with the experimental diets at both ...
Beta Amylase 150 slower - less body , , Alpha Amylase 158 faster - more body , , Dextrinase , , Beta Glucanase , , Mash-out 5 ... Alpha & Beta Acids * Essential Oils *Rhyzome - root cutting ____________________________________________________ , type alpha ...
Beta-Amylase activity and thermostability in wild and cultivated barleys with different Bmy1 intron III alleles (Abstract Only ... Barley and oat beta-glucan content measured by calcofluor fluorescence in a microplate assay (Abstract Only) (18-Aug-08) ... Calcofluor fluorescence assay for wort beta-glucan in a microplate format (Peer Reviewed Journal) (12-May-08) ... Fluorescence microplate readers as an alternative to flow injection analysis for determination of wort beta-glucan (Abstract ...
The optimal pH for alpha amylase is 5.3-5.7 while the optimal range for beta amylase is 5.1-5.3. Adding acid, calcium ions, or ... A thicker mash can add some temperature insulation for the beta amylase, while a thinner mash will result in alpha amylase ... If you are planning on mashing at a higher temperature, then you could opt to do a beta amylase rest within the enzymes ... It is typically active between131 and 149 °F. As your mash approaches 149 °F, the beta amylase is working at its fastest, but ...
It goes to work by inhibiting the digestive enzyme, alpha-amylase. By inhibiting the ability of this enzyme, you stop the ... beta glucans - which boost the immune system,. *and ultra-long-chain carbohydrates giving a slow, ...
beta-amylases and their roles in leaf starch metabolism. *Dana Moseley *Animal behavior, urban ecology, animal communication of ...
Another patent (EP332027B1) covers the beta-amylase modification of native starch to enhance their emulsifying action. ... Oat Beta-glucan - Clean Label Texturizer Content provided by Lantmännen Biorefineries AB , 21-Nov-2023 , White Paper ... Oat Beta-glucan - Clean Label Texturizer Lantmännen Biorefineries AB , Download Technical / White Paper ... For example, patented amylase enzymes from Novozymes have been used to improve the functionality of modified starch. ...
Amylase A group of enzymes (alpha amylase, beta amylase) present in most malted grains which are responsible for converting ... Alpha amylase One of the two primary enzymes responsible for breaking starch down into sugar. Alpha amylase is most active in ... Simple dextrins, from the reduction of starch by alpha amylase. Negative reaction with iodine. ... Amylase enzymes Enzymes which convert starches to sugars. See also: alpha amylase, beta amylase.. ...
Amylase A group of enzymes (alpha amylase, beta amylase) present in most malted grains which are responsible for converting ... Alpha amylase One of the two primary enzymes responsible for breaking starch down into sugar. Alpha amylase is most active in ... Simple dextrins, from the reduction of starch by alpha amylase. Negative reaction with iodine. ... Amylase enzymes Enzymes which convert starches to sugars. See also: alpha amylase, beta amylase.. ...
Dextrine malt contains a high percentage of dextrins which are unfermentable by the malt enzymes, alpha and beta amylase. No ...
and become accessible to amylases. Beta-amylases will cleave off maltose from starch molecules. The mash is then heated to 72°C ... groups of enzymes are activated: (i) amylases, (ii) proteases/peptidases, and (iii) beta-glucanases. Each of these enzymes have ... further breakdown of long chain polysaccharides by alpha-amylases. Finally, the temperature of the mash is raised to 78°C, ... peptidases break down proteins and release free amino nitrogen (FAN), while (iii) beta-glucanases degrade the endosperm cell ...
1.harga dan spesifikasi bahan kimia bioetanol (Enzym Alfa Amylase, Enzym Beta Amylase, Ragi Bioethanol);. 2.harga dan ...
Screening for alpha and beta Amylases were carried out in one hundred malted Nigerian maize cultivars. The trend of secretions ... of alpha and beta amylases was observed for eleven day germination period. Results obtained showed that third to fifth day ... Influence of malting time on α and β Amylases secretions in Nigerian Amylolytic maize Cultivars ...
One of SPBF binding site (SP8a); Found at -155 of gSPO-A1 (sporamin) gene, and also at -880 of gB-Amy (beta-amylase) gene in ... upstream region of three differnt genes coding for sporamin and beta-amylase; Binding site of SPF1; SPF1 also binds to the SP8b ... PolyA signal; poly A signal found in legA gene of pea, rice alpha-amylase; -10 to -30 in the case of animal genes. Near ... PolyA signal; poly A signal found in rice alpha-amylase; -10 to -30 in the case of animal genes. ...
Fazekas E, Szabo K, Kandra L, Gyemant G: Unexpected mode of action of sweet potato beta-amylase on maltooligomer substrates., ... Lehoczki G, Kandra L, Gyémánt G: The use of starch azure for measurement of alpha-amylase activity, CARBOHYDRATE POLYMERS 183: ... Szabo Karmen, Hamori Csaba, Gyemant Gyongyi: Gallotannins are non-specific inhibitors of alpha-amylase: Aggregates are the ... Hámori C., Remenyik J., Kandra L., Gyémánt G.: Colorado potato beetle alpha-amylase: Purification, action pattern and subsite ...
Beta-amylase. Allergenicity:. no information found. Route of allergen exposure:. Food. Date Created:. 27-10-2003. ...
Which is what leads me to this question of a beta-glucans rest before heading on to the amylase ranges. ... What I would call mash-out temp, as all amylases would be completely denatured at that temp. That said, it doesnt take 3 hours ... Has anyone thought of a beta-glucans rest during the mashing process, to untangle some of the gums formed (prior, and) during ... When I asked him about a higher temp, into a-amylase optima, he said avoid it, the dextrins lead to "gumminess". ...
The oldest criteria for linearity consisted in the susceptibility of the molecule to complete hydrolysis by beta-amylase. This ... When degraded by pure beta-amylase, linear macromolecules are completely converted into maltose, whereas branched chains give ... also one beta-limit dextrin consisting of the remaining inner core polysaccharide structure with its outer chains recessed. ... enzyme splits the (1→4) bonds from the non-reducing end of a chain releasing beta-maltosyl units, but cannot cleave the (1→6) ...
  • Amylase is a type of enzymes which is made-up of proteins, whose activity basically depends on their shapes and structures. (assignmenthelp.net)
  • Waits another 10 seconds…* For the 3 of you that stayed and decided that you are in for the long haul, we are going to be learning about amylase enzymes and the roles they play in the brewing process. (morebeer.com)
  • When it comes to brewing, amylase enzymes play a major role in the mashing process. (morebeer.com)
  • There are several different amylase enzymes, including ptyalin, which is an amylase enzyme present in your saliva that begins the digestion process by breaking down some simple starches (this is largely the reason why things like crackers will break down and dissolve in your mouth). (morebeer.com)
  • In the mash, we are really concerned with two main enzymes: alpha and beta amylase. (morebeer.com)
  • The last way that we can affect these enzyme actions is by adding commercially available, food-grade amylase enzymes directly to the mash. (morebeer.com)
  • Adding amylase enzymes to your mash will increase the rates of these reactions by providing more enzymes to break down sugars before total denaturation occurs. (morebeer.com)
  • Adding amylase enzymes can be helpful when brewing a beer that utilizes a large percentage of specialty malts that have been kilned at high enough temperature to denature most of the natural amylase enzymes typically found in barley. (morebeer.com)
  • For example, patented amylase enzymes from Novozymes have been used to improve the functionality of modified starch. (foodnavigator.com)
  • to investigate the activity of two major degrading enzymes - amylases and cellulase during fruit maturation and ripening. (omicsonline.org)
  • Amylases (which include both alpha amylase and beta amylase) are the major category of starch degrading enzymes and cellulase is responsible for the cell wall (cellulose) degradation in fruit tissue that results in tissue softening. (omicsonline.org)
  • The principal enzymes responsible for starch conversion are alpha- and beta-amylase. (beer-brewing.com)
  • Amylases are starch hydrolyzing enzymes which are classified as exo-amylase and endo-amylase that act on α-1,4- and α-1,6-glucosidic bonds of starch and glycogen. (biosynsis.com)
  • Magnitude of Changes in the Activity of Amylases and Cellulase and its Association with the Biochemical Composition during Maturation and Ripening of Banana (Musa spp. (omicsonline.org)
  • Specific activities of amylases and cellulase were analyzed by standard assay procedures. (omicsonline.org)
  • Results and discussion: Significant variations in the specific activity of amylases and cellulase were observed between different periods of maturity. (omicsonline.org)
  • The activity of amylase and cellulase had significant correlations with the concentrations of related biochemical constituents such as starch and cellulose. (omicsonline.org)
  • The present research work was focused on the isolation and partial characterization of soil bacteria that can produce amylase, cellulase, lipase, and proteases. (researchbib.com)
  • Crystal Structure of a Beta-Amylase from Bacillus cereus var. (expasy.org)
  • In these days amylase is produced by bacteria called Bacillus amyloliquefaciens P-001. (assignmenthelp.net)
  • Amylase is divided in three types : a) Alpha-amylase, b) Beta-amylase, and c) Gamma-amylase. (assignmenthelp.net)
  • Beta and gamma amylase are not found in animal tissue. (assignmenthelp.net)
  • A form of amylase found in bacteria , molds, yeast s, and the seed s of plants that cuts alpha-bonds of large sugar molecules (e.g. starch, glycogen , and related polysaccharide s), removing the successive beta-maltose units from the non-reducing ends of the chains. (biologyonline.com)
  • One Unit of β-amylase activity is defined as the amount of enzyme required to release one µmole of maltose reducing-sugar equivalents per minute from soluble starch (10 mg/mL) in sodium phosphate buffer (200 mM), pH 6.0 at 40°C. (neogen.com)
  • It catalyses the following reaction: Hydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains This enzyme acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion. (wikipedia.org)
  • Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. (wikipedia.org)
  • When degraded by pure beta-amylase, linear macromolecules are completely converted into maltose, whereas branched chains give also one beta-limit dextrin consisting of the remaining inner core polysaccharide structure with its outer chains recessed. (hmdb.ca)
  • Together, alpha- and beta-amylase are capable of converting only 60 to 80 percent of the available starch to fermentable sugars, which is mostly maltose and maltotriose (Dougherty, 1977). (beer-brewing.com)
  • β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. (wikipedia.org)
  • The following are the amylase-producing microorganisms including bacteria and fungi that we are capable of developing as synthetic biology chassis. (biosynsis.com)
  • In plants, the β-amylase breaks starch into sugar , resulting in the sweet flavor of ripe fruit. (biologyonline.com)
  • Supplement In plants, the β-amylase breaks starch into sugar, resulting in the. (biologyonline.com)
  • However they are often annotated in the NCBI protein database as the DUF1551 or PF04314 family, alpha-amylase catalytic proteins, members of the Phenol_MetA-deg (MetA-pathway of phenol degradation) superfamily, signal peptide proteins and porins. (tcdb.org)
  • Protein engineering of amylases to improve their catalytic activity, substrate specificity, thermostability, and pH tolerance. (biosynsis.com)
  • Powder enzyme form (2000°L) is for use in AACC and ASBC α-amylase assay procedures (see E-BARBP). (neogen.com)
  • For use in AACC and ASBC α-amylase assay procedures. (neogen.com)
  • The oldest criteria for linearity consisted in the susceptibility of the molecule to complete hydrolysis by beta-amylase. (hmdb.ca)
  • We can use powerful synthetic biology tools to specifically modify amylases to improve enzyme activity. (biosynsis.com)
  • These are the proteins and binds with active site of amylase, it is nutritional supplements. (assignmenthelp.net)
  • The BBP/AA family consists of proteins predicted to consist of outer membane beta-barrels. (tcdb.org)
  • A study found that if you keep laboratory rats on fructose long enough they get tau and amyloid beta proteins in the brain, the same proteins seen in Alzheimer's disease," Johnson said. (hypothes.is)
  • The proteins synthesized by parotid acinar cells are stored in large secretory granules whose composition includes α-amylase, leucine-rich parotid secretory protein (PSP), and proline-rich proteins (PRPs), in addition to multiple minor components 2-3 related to digestive and protective functions. (bvsalud.org)
  • β-amylase is present in an inactive form prior to seed germination. (wikipedia.org)
  • Unexpected mode of action of sweet potato beta-amylase on maltooligomer substrates. (doktori.hu)
  • Sour cherry extract inhibits human salivary α-amylase and growth of Streptococcus mutans (a pilot clinical study) , FOOD AND FUNCTION 9: (7) pp. 4008-4016. (doktori.hu)
  • Simple ITC method for activity and inhibition studies on human salivary α-amylase , JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY 31: (6) pp. 1648-1653. (doktori.hu)
  • Biochemical properties such as production of alpha-amylase, beta-glucosidase, tannase, antimicrobials (presumptive bacteriocin and H(2)O(2)-production), acidification and fermentation of the indigestible sugars raffinose and stachyose, were evaluated in vitro for selection of potential starter strains. (who.int)
  • Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. (wikipedia.org)
  • Recent advances in synthetic biology have led to breakthroughs in the development of high-quality amylase-producing microorganisms through genetic and metabolic engineering strategies. (biosynsis.com)
  • Isolation, identification, and selection of amylase-producing microorganisms with the potential to produce highly active amylases. (biosynsis.com)
  • Engineering of amylase-producing microorganisms to achieve high production potentials for a wide range of industrial applications. (biosynsis.com)
  • Amylase-producing microorganisms. (biosynsis.com)
  • Our expertise and advanced technologies in bacterial synthetic biology, fungal synthetic biology and algal synthetic biology allow us to develop effective genetic tools and metabolic engineering strategies that enable different types of microorganisms to obtain desirable properties and become ideal chassis for the production of amylases suitable for different application scenarios. (biosynsis.com)
  • It is typically active between131 and 149 °F. As your mash approaches 149 °F, the beta amylase is working at its fastest, but it is also denaturing rapidly. (morebeer.com)
  • A lower temperature mash will create more beta amylase, which will create a wort that is more fermentable, but may yield slightly less extract and have less body. (morebeer.com)
  • If you are aiming for a mash temperature above 149 and you utilize a single-infusion mash, then you run the risk of denaturing the beta amylase very quickly and diminishing its effects. (morebeer.com)
  • Mash thickness can also play a role in amylase enzyme action. (morebeer.com)
  • A thicker mash can add some temperature insulation for the beta amylase, while a thinner mash will result in alpha amylase being more prominent. (morebeer.com)
  • As you transitioned through the mash cyle from the beta to alpha amylase active periods, the starch chains are reduced in defferent ways with the beta amylase working on the shorter branches from 130-150F whereas the alpha amylase reduces the larger trunk ends of the starch chains from 152-162 converting them into the sugars sytematically as the mash progresses through the temp cycle. (homebrewersassociation.org)
  • Beta-amylase is the other mash enzyme capable of degrading starch. (beer-brewing.com)
  • So, given that alpha- and beta-amylase have different optimum temperatures the brewer will often slowly ramp the temperature of the mash from 50 to 78 degrees C (120-172°F). This ensures that each enzyme becomes activated at its optimum temperature as the process ensues. (beer-brewing.com)
  • Gallotannins are non-specific inhibitors of alpha-amylase: Aggregates are the active species taking part in inhibition , CHEMICAL BIOLOGY & DRUG DESIGN 97: (2) pp. 349-357. (doktori.hu)
  • Beta-amylase activity. (joplink.net)
  • The use of starch azure for measurement of alpha-amylase activity , CARBOHYDRATE POLYMERS 183: pp. 263-266. (doktori.hu)
  • The activity of amylases was found to be very low (4.8 ± 0.26 Units) during the tender stage, remained low up to 90th days (14.00 ± 0.86 Units) of maturation, but when the fruits starts ripening after 90 days it increased to about 10 folds on the 92nd day (103.40 ± 8.20 Units) and then gradually decreased towards the overripe stage ie. (omicsonline.org)
  • Activity of α-amylase and α-glucosidase was inhibited by extracts of all S. spinosum organs. (biomedcentral.com)
  • Alpha amylase is responsible for breaking down large, complex, insoluble starch molecules into smaller, soluble molecules. (morebeer.com)
  • Alpha-amylase very rapidly reduces insoluble and soluble starch by splitting complex starch molecules into many shorter chains (i.e., partially-fermentable polysaccharide fractions-dextrins and maltotriose) that can be attacked by beta-amylase. (beer-brewing.com)
  • This enzyme splits the (1→4) bonds from the non-reducing end of a chain releasing beta-maltosyl units, but cannot cleave the (1→6) bonds. (hmdb.ca)
  • The level of alpha amylase in bread making must be sufficient to produce saccharides, which is used by yeast. (assignmenthelp.net)
  • Then we can only discus about Alpha- amylase, which play an important role in digestive and metabolic process. (assignmenthelp.net)
  • It will convert starch to soluble sugars in a temperature range from 145 to 158 °F. Beta amylase is mostly responsible for creating large amounts of fermentable sugar. (morebeer.com)
  • If you are planning on mashing at a higher temperature, then you could opt to do a beta amylase rest within the enzyme's optimal temperature range to increase the wort's fermentability before raising the temperature into alpha amylase's optimal temperature range. (morebeer.com)
  • The level of alpha-amylase in brewing industries is a key quality parameters. (assignmenthelp.net)
  • We work to enhance the physical and chemical parameters of amylases for industrial use through synthetic biology in order to break the limitations of amylases in practical applications. (biosynsis.com)
  • The beta subunit is the same in both the muscle and hepatic isoforms, and encoded by one gene. (nih.gov)
  • Keywords 「alpha and beta amylase」 match 89 products. (glucoamylaseenzyme.com)
  • Screening for alpha and beta Amylases were carried out in one hundred malted Nigerian maize cultivars. (academicjournals.org)
  • The trend of secretions of alpha and beta amylases was observed for eleven day germination period. (academicjournals.org)
  • The gamma subunits contain the active site of the enzyme, whereas the alpha and beta subunits have regulatory functions controlled by phosphorylation. (nih.gov)
  • In prolonged fasting, the brain derives a large portion of its oxidative energy from the ketone bodies, beta-hydroxybutyrate and acetoacetate, thereby reducing whole body glucose consumption. (hypothes.is)
  • Beta-amylase is more selective than alpha-amylase since it breaks off two sugars at a time from the starch chain. (beer-brewing.com)
  • The optimum pH for β-amylase is 4.0-5.0 They belong to Glycoside hydrolase family 14. (wikipedia.org)
  • Colorado potato beetle alpha-amylase: Purification, action pattern and subsite mapping for exploration of active centre , INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 168: pp. 350-355. (doktori.hu)
  • In cereals grains and their products, level of alpha amylase is significantly affected by industrial exploitation of these commodity. (assignmenthelp.net)
  • Synthetic biology provides new ways to significantly improve the functional specificity and enzyme stability of amylases, thus helping to achieve large-scale, efficient, and ultra-environmentally friendly industrial production of amylases. (biosynsis.com)
  • Usually a single infusion at 156F means you are aiming for a beer with more body and a sweeter finish, since this temp favors the alpha amylase which makes starch into big chunks that aren't all fermentable. (homebrewersassociation.org)
  • We can help develop strategies for mutagenesis and cloning to produce engineered amylases with improved functionality and stability. (biosynsis.com)
  • Many microbes also produce amylase to degrade extracellular starches. (wikipedia.org)