Apoproteins: The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).Apolipoproteins: Protein components on the surface of LIPOPROTEINS. They form a layer surrounding the hydrophobic lipid core. There are several classes of apolipoproteins with each playing a different role in lipid transport and LIPID METABOLISM. These proteins are synthesized mainly in the LIVER and the INTESTINES.Lipoproteins, HDL: A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases.Lipoproteins, VLDL: A class of lipoproteins of very light (0.93-1.006 g/ml) large size (30-80 nm) particles with a core composed mainly of TRIGLYCERIDES and a surface monolayer of PHOSPHOLIPIDS and CHOLESTEROL into which are imbedded the apolipoproteins B, E, and C. VLDL facilitates the transport of endogenously made triglycerides to extrahepatic tissues. As triglycerides and Apo C are removed, VLDL is converted to INTERMEDIATE-DENSITY LIPOPROTEINS, then to LOW-DENSITY LIPOPROTEINS from which cholesterol is delivered to the extrahepatic tissues.Lipoproteins: Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes.Egg Proteins, Dietary: Proteins found in eggs which are consumed as a food.Chylomicrons: A class of lipoproteins that carry dietary CHOLESTEROL and TRIGLYCERIDES from the SMALL INTESTINE to the tissues. Their density (0.93-1.006 g/ml) is the same as that of VERY-LOW-DENSITY LIPOPROTEINS.Apolipoproteins A: Structural proteins of the alpha-lipoproteins (HIGH DENSITY LIPOPROTEINS), including APOLIPOPROTEIN A-I and APOLIPOPROTEIN A-II. They can modulate the activity of LECITHIN CHOLESTEROL ACYLTRANSFERASE. These apolipoproteins are low in atherosclerotic patients. They are either absent or present in extremely low plasma concentration in TANGIER DISEASE.Immunoelectrophoresis: A technique that combines protein electrophoresis and double immunodiffusion. In this procedure proteins are first separated by gel electrophoresis (usually agarose), then made visible by immunodiffusion of specific antibodies. A distinct elliptical precipitin arc results for each protein detectable by the antisera.Blood Protein DisordersLight-Harvesting Protein Complexes: Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.Lymph: The interstitial fluid that is in the LYMPHATIC SYSTEM.Apolipoproteins B: Major structural proteins of triacylglycerol-rich LIPOPROTEINS. There are two forms, apolipoprotein B-100 and apolipoprotein B-48, both derived from a single gene. ApoB-100 expressed in the liver is found in low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). ApoB-48 expressed in the intestine is found in CHYLOMICRONS. They are important in the biosynthesis, transport, and metabolism of triacylglycerol-rich lipoproteins. Plasma Apo-B levels are high in atherosclerotic patients but non-detectable in ABETALIPOPROTEINEMIA.Lipoproteins, LDL: A class of lipoproteins of small size (18-25 nm) and light (1.019-1.063 g/ml) particles with a core composed mainly of CHOLESTEROL ESTERS and smaller amounts of TRIGLYCERIDES. The surface monolayer consists mostly of PHOSPHOLIPIDS, a single copy of APOLIPOPROTEIN B-100, and free cholesterol molecules. The main LDL function is to transport cholesterol and cholesterol esters to extrahepatic tissues.Apolipoprotein A-I: The most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. This protein serves as an acceptor for CHOLESTEROL released from cells thus promoting efflux of cholesterol to HDL then to the LIVER for excretion from the body (reverse cholesterol transport). It also acts as a cofactor for LECITHIN CHOLESTEROL ACYLTRANSFERASE that forms CHOLESTEROL ESTERS on the HDL particles. Mutations of this gene APOA1 cause HDL deficiency, such as in FAMILIAL ALPHA LIPOPROTEIN DEFICIENCY DISEASE and in some patients with TANGIER DISEASE.Ultracentrifugation: Centrifugation with a centrifuge that develops centrifugal fields of more than 100,000 times gravity. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Apolipoprotein A-II: The second most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. It has a high lipid affinity and is known to displace APOLIPOPROTEIN A-I from HDL particles and generates a stable HDL complex. ApoA-II can modulate the activation of LECITHIN CHOLESTEROL ACYLTRANSFERASE in the presence of APOLIPOPROTEIN A-I, thus affecting HDL metabolism.Chlorophyll: Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.Hordeum: A plant genus of the family POACEAE. The EDIBLE GRAIN, barley, is widely used as food.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Apolipoproteins C: A group of apolipoproteins that can readily exchange among the various classes of lipoproteins (HDL; VLDL; CHYLOMICRONS). After lipolysis of TRIGLYCERIDES on VLDL and chylomicrons, Apo-C proteins are normally transferred to HDL. The subtypes can modulate remnant binding to receptors, LECITHIN CHOLESTEROL ACYLTRANSFERASE, or LIPOPROTEIN LIPASE.Tetranitromethane: Corrosive oxidant, explosive; additive to diesel and rocket fuels; causes skin and lung irritation; proposed war gas. A useful reagent for studying the modification of specific amino acids, particularly tyrosine residues in proteins. Has also been used for studying carbanion formation and for detecting the presence of double bonds in organic compounds.Lipoproteins, HDL3: Intermediate-density subclass of the high-density lipoproteins, with particle sizes between 7 to 8 nm. As the larger lighter HDL2 lipoprotein, HDL3 lipoprotein is lipid-rich.Dimethyl Suberimidate: The methyl imidoester of suberic acid used to produce cross links in proteins. Each end of the imidoester will react with an amino group in the protein molecule to form an amidine.TriglyceridesPhotosynthetic Reaction Center Complex Proteins: Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.Imidoesters: Esters of the hypothetical imidic acids. They react with amines or amino acids to form amidines and are therefore used to modify protein structures and as cross-linking agents.Pulmonary Surfactant-Associated Proteins: Proteins found in the LUNG that act as PULMONARY SURFACTANTS.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.Chlorophyll Binding Proteins: A large family of proteins that have been traditionally classified as the light-harvesting proteins of the photosynthetic reaction complex. Chlorophyll binding proteins are also found in non-photosynthetic settings where they may play a photoprotective role in response to light stress.Complement C9: A 63-kDa serum glycoprotein encoded by gene C9. Monomeric C9 (mC9) binds the C5b-8 complex to form C5b-9 which catalyzes the polymerization of C9 forming C5b-p9 (MEMBRANE ATTACK COMPLEX) and transmembrane channels leading to lysis of the target cell. Patients with C9 deficiency suffer from recurrent bacterial infections.Apolipoprotein C-III: A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS and CHYLOMICRON REMNANTS. Apo C-III, synthesized in the liver, is an inhibitor of LIPOPROTEIN LIPASE. Apo C-III modulates the binding of chylomicron remnants and VLDL to receptors (RECEPTORS, LDL) thus decreases the uptake of triglyceride-rich particles by the liver cells and subsequent degradation. The normal Apo C-III is glycosylated. There are several polymorphic forms with varying amounts of SIALIC ACID (Apo C-III-0, Apo C-III-1, and Apo C-III-2).Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Hypolipoproteinemias: Conditions with abnormally low levels of LIPOPROTEINS in the blood. This may involve any of the lipoprotein subclasses, including ALPHA-LIPOPROTEINS (high-density lipoproteins); BETA-LIPOPROTEINS (low-density lipoproteins); and PREBETA-LIPOPROTEINS (very-low-density lipoproteins).Apolipoprotein C-II: A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS. It contains a cofactor for LIPOPROTEIN LIPASE and activates several triacylglycerol lipases. The association of Apo C-II with plasma CHYLOMICRONS; VLDL, and HIGH-DENSITY LIPOPROTEINS is reversible and changes rapidly as a function of triglyceride metabolism. Clinically, Apo C-II deficiency is similar to lipoprotein lipase deficiency (HYPERLIPOPROTEINEMIA TYPE I) and is therefore called hyperlipoproteinemia type IB.Aurintricarboxylic Acid: A dye which inhibits protein biosynthesis at the initial stages. The ammonium salt (aluminon) is a reagent for the colorimetric estimation of aluminum in water, foods, and tissues.Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.Lipids: A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)Pulmonary Surfactants: Substances and drugs that lower the SURFACE TENSION of the mucoid layer lining the PULMONARY ALVEOLI.Pigments, Biological: Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms.Chloroplasts: Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.Apolipoproteins E: A class of protein components which can be found in several lipoproteins including HIGH-DENSITY LIPOPROTEINS; VERY-LOW-DENSITY LIPOPROTEINS; and CHYLOMICRONS. Synthesized in most organs, Apo E is important in the global transport of lipids and cholesterol throughout the body. Apo E is also a ligand for LDL receptors (RECEPTORS, LDL) that mediates the binding, internalization, and catabolism of lipoprotein particles in cells. There are several allelic isoforms (such as E2, E3, and E4). Deficiency or defects in Apo E are causes of HYPERLIPOPROTEINEMIA TYPE III.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Photosystem I Protein Complex: A large multisubunit protein complex that is found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to drive electron transfer reactions that result in either the reduction of NADP to NADPH or the transport of PROTONS across the membrane.Phycocyanin: The metal-free blue phycobilin pigment in a conjugated chromoprotein of blue-green algae. It functions as light-absorbing substance together with chlorophylls.Cholesterol Esters: Fatty acid esters of cholesterol which constitute about two-thirds of the cholesterol in the plasma. The accumulation of cholesterol esters in the arterial intima is a characteristic feature of atherosclerosis.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Immunodiffusion: Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.Photosystem II Protein Complex: A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN.Hyperlipoproteinemias: Conditions with abnormally elevated levels of LIPOPROTEINS in the blood. They may be inherited, acquired, primary, or secondary. Hyperlipoproteinemias are classified according to the pattern of lipoproteins on electrophoresis or ultracentrifugation.Molecular Weight: The sum of the weight of all the atoms in a molecule.Cholesterol, Dietary: Cholesterol present in food, especially in animal products.Kinetics: The rate dynamics in chemical or physical systems.Phytochrome: A blue-green biliprotein widely distributed in the plant kingdom.Iron-Sulfur Proteins: A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.Complement Membrane Attack Complex: A product of COMPLEMENT ACTIVATION cascade, regardless of the pathways, that forms transmembrane channels causing disruption of the target CELL MEMBRANE and cell lysis. It is formed by the sequential assembly of terminal complement components (COMPLEMENT C5B; COMPLEMENT C6; COMPLEMENT C7; COMPLEMENT C8; and COMPLEMENT C9) into the target membrane. The resultant C5b-8-poly-C9 is the "membrane attack complex" or MAC.Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Perfusion: Treatment process involving the injection of fluid into an organ or tissue.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Apoenzymes: The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.Light: That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.Centrifugation, Density Gradient: Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Carbon-Carbon Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.Lipoprotein Lipase: An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and diacylglycerols. It occurs on capillary endothelial surfaces, especially in mammary, muscle, and adipose tissue. Genetic deficiency of the enzyme causes familial hyperlipoproteinemia Type I. (Dorland, 27th ed) EC 3.1.1.34.Immunosorbent Techniques: Techniques for removal by adsorption and subsequent elution of a specific antibody or antigen using an immunosorbent containing the homologous antigen or antibody.Rats, Inbred Strains: Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Cholesterol, VLDL: Cholesterol which is contained in or bound to very low density lipoproteins (VLDL). High circulating levels of VLDL cholesterol are found in HYPERLIPOPROTEINEMIA TYPE IIB. The cholesterol on the VLDL is eventually delivered by LOW-DENSITY LIPOPROTEINS to the tissues after the catabolism of VLDL to INTERMEDIATE-DENSITY LIPOPROTEINS, then to LDL.Hyperlipidemias: Conditions with excess LIPIDS in the blood.Darkness: The absence of light.Radioimmunoassay: Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Cholesterol, HDL: Cholesterol which is contained in or bound to high-density lipoproteins (HDL), including CHOLESTEROL ESTERS and free cholesterol.Phosphatidylcholines: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Molecular Sequence Data: 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.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Dietary Fats: Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.Spectrum Analysis: The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Cholesterol, LDL: Cholesterol which is contained in or bound to low density lipoproteins (LDL), including CHOLESTEROL ESTERS and free cholesterol.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

The binding of human lactoferrin to mouse peritoneal cells. (1/1461)

Human iron-saturated Lf (FeLf), which was labeled with 125I or 50Fe, was found to combine with the membrane of mouse peritoneal cells (MPC) which consisted of 70% macrophages. The following experimental data suggested the involvement of a specific receptor. (a) The binding of FeLf to MPC reached a saturation point. (b) The binding of radioactive FeLf was inhibited by preincubating the cells with cold FeLf but not with human Tf, human aggregated and nonaggregated IgG, or beef heart cytochrome c (c) Succinylation and carbamylation of FeLf resulted in a loss of its inhibiting activity on the binding of radioactive FeLf. Removal of neuraminic acid from FeLf increased its inhibitory activity. (d) The ability of apoLf to inhibit the binding of FeLf to MPC was significantly lower than that of FeLf. The existence of a Lf receptor capable of concentrating Lf released from neutrophils on the membrane of macrophages could explain the apparent blockade of the release of iron from the reticuloendothelial system, which accounts for the hyposideremia of inflammation. A receptor for FeLf was also found on mouse peritoneal lymphocytes. The affinity constant of FeLf for both lymphocytes and macrophages was 0.9 X 12(6) liter/mol. Howerver, macrophages bound three times more FeLf molecules (20 X 10(6)) per cell than did lymphocytes (7 X 10(6)).  (+info)

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state. (2/1461)

Unfolded apocytochrome c acquires an alpha-helical conformation upon interaction with lipid. Folding kinetic results below and above the lipid's CMC, together with energy transfer measurements of lipid bound states, and salt-induced compact states in solution, show that the folding transition of apocytochrome c from the unfolded state in solution to a lipid-inserted helical conformation proceeds via a collapsed intermediate state (I(C)). This initial compact state is driven by a hydrophobic collapse of the polypeptide chain in the absence of the heme group and may represent a heme-free analogue of an early compact intermediate detected on the folding pathway of cytochrome c in solution. Insertion into the lipid phase occurs via an unfolding step of I(C) through a more extended state associated with the membrane surface (I(S)). While I(C) appears to be as compact as salt-induced compact states in solution with substantial alpha-helix content, the final lipid-inserted state (Hmic) is as compact as the unfolded state in solution at pH 5 and has an alpha-helix content which resembles that of native cytochrome c.  (+info)

Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. (3/1461)

On exposure to mildly acidic conditions, apomyoglobin forms a partially folded intermediate, I. The A, B, G, and H helices are significantly structured in this equilibrium intermediate, whereas the remainder of the protein is largely unfolded. We report here the effects of mutations at helix pairing sites on the stability of I in three classes of mutants that: (i) truncate hydrophobic side chains in native helix packing sites, (ii) truncate hydrophobic side chains not involved in interhelical contacts, and (iii) extend hydrophobic side chains at residues not involved in interhelical contacts. Class I mutants significantly decrease the stability and cooperativity of folding of the intermediate. Class II and III mutants show smaller effects on stability and have little effect on cooperativity. Qualitatively similar results to those found in I were obtained for all three classes of mutants in native myoglobin (N), demonstrating that hydrophobic burial is fairly specific to native helix packing sites in I as well as in N. These results suggest that hydrophobic burial along native-like interhelical contacts is important for the formation of the cooperatively folded intermediate.  (+info)

Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: application to the 10-55 fragment of staphylococcal protein A and to apo calbindin D9K. (4/1461)

The conformational space annealing (CSA) method for global optimization has been applied to the 10-55 fragment of the B-domain of staphylococcal protein A (protein A) and to a 75-residue protein, apo calbindin D9K (PDB ID code), by using the UNRES off-lattice united-residue force field. Although the potential was not calibrated with these two proteins, the native-like structures were found among the low-energy conformations, without the use of threading or secondary-structure predictions. This is because the CSA method can find many distinct families of low-energy conformations. Starting from random conformations, the CSA method found that there are two families of low-energy conformations for each of the two proteins, the native-like fold and its mirror image. The CSA method converged to the same low-energy folds in all cases studied, as opposed to other optimization methods. It appears that the CSA method with the UNRES force field, which is based on the thermodynamic hypothesis, can be used in prediction of protein structures in real time.  (+info)

Thermodynamic studies on anion binding to apotransferrin and to recombinant transferrin N-lobe half molecules. (5/1461)

Equilibrium constants for the binding of anions to apotransferrin, to the recombinant N-lobe half transferrin molecule (Tf/2N), and to a series of mutants of Tf/2N have been determined by difference UV titrations of samples in 0.1 M Hepes buffer at pH 7.4 and 25 degrees C. The anions included in this study are phosphate, sulfate, bicarbonate, pyrophosphate, methylenediphosphonic acid, and ethylenediphosphonic acid. There are no significant differences between anion binding to Tf/2N and anion binding to the N-lobe of apotransferrin. The binding of simple anions like phosphate appears to be essentially equivalent for the two apotransferrin binding sites. The binding of pyrophosphate and the diphosphonates is inequivalent, and the studies on the recombinant Tf/2N show that the stronger binding is associated with the N-terminal site. Anion binding constants for phosphate, pyrophosphate, and the diphosphonates with the N-lobe mutants K206A, K296A, and R124A have been determined. Anion binding tends to be weakest for the K296A mutant, but the variation in log K values among the three mutants is surprisingly small. It appears that the side chains of K206, K296, and R124 all make comparable contributions to anion binding. There are significant variations in the intensities of the peaks in the difference UV spectra that are generated by the titrations of the mutant apoproteins with these anions. These differences appear to be related more to variations in the molar extinction coefficients of the anion-protein complexes rather than to differences in binding constants.  (+info)

Suppressor analysis of mutations in the 5'-untranslated region of COB mRNA identifies components of general pathways for mitochondrial mRNA processing and decay in Saccharomyces cerevisiae. (6/1461)

The cytochrome b gene in Saccharomyces cerevisiae, COB, is encoded by the mitochondrial genome. Nuclear-encoded Cbp1 protein is required specifically for COB mRNA stabilization. Cbp1 interacts with a CCG element in a 64-nucleotide sequence in the 5'-untranslated region of COB mRNA. Mutation of any nucleotide in the CCG causes the same phenotype as cbp1 mutations, i.e., destabilization of both COB precursor and mature message. In this study, eleven nuclear suppressors of single-nucleotide mutations in CCG were isolated and characterized. One dominant suppressor is in CBP1, while the other 10 semidominant suppressors define five distinct linkage groups. One group of four mutations is in PET127, which is required for 5' end processing of several mitochondrial mRNAs. Another mutation is linked to DSS1, which is a subunit of mitochondrial 3' --> 5' exoribonuclease. A mutation linked to the SOC1 gene, previously defined by recessive mutations that suppress cbp1 ts alleles and stabilize many mitochondrial mRNAs, was also isolated. We hypothesize that the products of the two uncharacterized genes also affect mitochondrial RNA turnover.  (+info)

Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate. (7/1461)

Folding of apomyoglobin is characterized by formation of a compact intermediate that contains substantial helicity. To determine whether this intermediate is obligatory or whether the protein can fold directly into the native state via an alternate parallel pathway, we have combined quench-flow hydrogen-exchange pulse labeling techniques with electrospray ionization mass spectrometry. The mass spectra of apomyoglobin obtained at various refolding times suggest that apomyoglobin indeed folds through a single pathway containing an obligatory intermediate with a significant hydrogen-bonded secondary structure content.  (+info)

The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent. (8/1461)

We have performed a detailed study of methanol-induced conformational transitions of horse heart apomyoglobin (apoMb) to investigate the existence of the compact and expanded denatured states. A combination of far- and near-ultraviolet circular dichroism, NMR spectroscopy, and small-angle X-ray scattering (SAXS) was used, allowing a phase diagram to be constructed as a function of pH and the methanol concentration. The phase diagram contains four conformational states, the native (N), acid-denatured (U(A)), compact denatured (I(M)), and expanded helical denatured (H) states, and indicates that the compact denatured state (I(M)) is stable under relatively mild denaturing conditions, whereas the expanded denatured states (U(A) and H) are realized under extreme conditions of pH (strong electric repulsion) or alcohol concentration (weak hydrophobic interaction). The results of this study, together with many previous studies in the literature, indicate the general existence of the compact denatured states not only in the salt-pH plane but also in the alcohol-pH plane. Furthermore, to determine the general feature of the H conformation we used several proteins including ubiquitin, ribonuclease A, alpha-lactalbumin, beta-lactoglobulin, and Streptomyces subtilisin inhibitor (SSI) in addition to apoMb. SAXS studies of these proteins in 60% methanol showed that the H states of these all proteins have expanded and nonglobular conformations. The qualitative agreement of the experimental data with computer-simulated Kratky profiles also supports this structural feature of the H state.  (+info)

Methods of inhibiting bacterial adhesion to medical implants and reducing device-associated infection are effectuated by administering an effective amount of apo-transferrin to an individual with such an implant. Preferably the apo-transferrin is administered by controlled release at or near the implant.
Gentaur molecular products has all kinds of products like :search , Assaypro \ Apotransferrin, anti_human \ 12091-05015 for more molecular products just contact us
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Article: We report studies of the interaction of Alzheimers amyloid beta protein (Aβ) with normal human plasma high density lipoprotein (HDL), aiming to clarify to which lipoprotein (LP) structural constituent (apolipoprotein or lipid) soluble Aβ is primarily bound. Purified HDLs were incubated wit...
F. Hammett, S. Saltissi, S. Rao, N. Miller, J. Coltart, B. Lewis; Plasma Lipoprotein Subclasses and Apoproteins as Predictors of Coronary Atherosclerosis in Man. Clin Sci (Lond) 1 February 1980; 58 (2): 31P. doi: https://doi.org/10.1042/cs058031Pa. Download citation file:. ...
The protein encoded by this gene is a G-protein coupled receptor involved in the regulation of feeding behavior. The encoded protein binds the hypothalamic neuropeptides
E coli CcmH protein: a component of the putative CcmFH heme lyase complex involved in transfer of heme from CcmE to apocytochrome c; has been sequenced
The effect of iron on the exocytosis of transferrin by K562 cells was studied by first allowing the cells to endocytose apotransferrin or diferric transferrin. Subsequent release of the apotransferrin was very rapid with a t 1/2 of 3.01 min, compared with 5.5 min for diferric transferrin. Release of apotransferrin was slowed by the weak base methylamine, t 1/2 8.0 min, but the effect of this agent was substantially greater when iron-transferrin was used, t 1/2 18.65 min, suggesting that methylamine affects both iron removal and receptor recycling. Release of iron-transferrin could be accelerated to a rate comparable with that of apotransferrin by addition of the permeant iron-chelator desferrioxamine. The difference in the rates of release of different forms of the protein could be explained by the re-endocytosis of the iron-rich protein, a process detected by the accelerated release of transferrin when the cells were washed in medium at pH 5.5 containing an iron-chelator or treated with a ...
Apo Transferrin vs Human transferrin - posted in Cell Biology Products: Greetings, What is the difference between apo-transferrin and human transferrin? I got their definition of apo-transferrin is free from iron binding while transferrin based on Sigma product is already half-saturated with iron. Once saturated with iron, i.e forming holo-transferrin it will bring iron into cell by receptor binding of the cell. I am confused why Sigma need to have two different products which in th...
Erratum: PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin (Infection and Immunity (2004) 72, 9 (5031-5040 ...
Protein structures provide a valuable resource for rational drug design. For a protein with no known ligand, computational tools can predict surface pockets that are of suitable size and shape to accommodate a complementary small-molecule drug. However, pocket prediction against single static structures may miss features of pockets that arise from proteins dynamic behaviour. In particular, ligand-binding conformations can be observed as transiently populated states of the apo protein, so it is possible to gain insight into ligand-bound forms by considering conformational variation in apo proteins. This variation can be explored by considering sets of related structures: computationally generated conformers, solution NMR ensembles, multiple crystal structures, homologues or homology models. It is non-trivial to compare pockets, either from different programs or across sets of structures. For a single structure, difficulties arise in defining particular pockets boundaries. For a set of conformationally
The interaction between Np(V) and human aposerumtransferrin (apoTf) was studied in vitro under simulated physiological conditions (37°C, pH 7.4, [NaCl] = 0.15 M, [HEPES] = 5 × 10-2 M) by UV-visible and near-IR absorption spectrophotometry and by ultrafiltration. It was found that Np(V) was bound in small fraction (, 12%) to apoTf, and that the role of carbonate and citrate anions in binding is more competitive than synergistic. The complexes NpO2CO3- and NpO2Cit2- tend to form rather than the Np(V)-apoTf complex. Np(V) binding on apotransferrin appears to be pH-dependent and reversible. Displacement experiments with FeIIINTA showed non-specific binding, suggesting a weak interaction between Np(V) and apotransferrin different from the reactions involving transferrin-specific sites with other metallic ions, such as Fe(III). The low overall charge, the size and the geometry of the linear di-oxocation NpO2+ could account for the weak interaction between Np(V) and human transferrin ...
David Yue and colleagues report in the the current issue of Cell a surprising role for Ca2+-unbound apopcalmodulin in regulating calcium and sodium channel activities. The Ca2+-free form of calmodulin (apoCaM) often appears inert, modulating target molecules only upon conversion to its Ca2+-bound form. This schema has appeared to govern voltage-gated Ca2+ channels, where apoCaM has been considered a dormant Ca2+ sensor, associated with channels but awaiting the binding of Ca2+ ions before inhibiting channel opening to provide vital feedback inhibition. Using single-molecule measurements of channels and chemical dimerization to elevate apoCaM, we find that apoCaM binding on its own markedly upregulates opening, rivaling the strongest forms of modulation. Upon Ca2+ binding to this CaM, inhibition may simply reverse the initial upregulation. As RNA-edited and -spliced channel variants show different affinities for apoCaM, the apoCaM-dependent control mechanisms may underlie the functional diversity ...
Gentaur molecular products has all kinds of products like :search , SeraLab \ Australian Origin Bovine Transferrin _ HOLO \ BSA-006-1G for more molecular products just contact us
Population fI of the molten globule state of apomyoglobin mutants.Dependency of the population fI of the molten globule state versus urea concentration for apom
Hi folks Iv just phoned to get some results of blood samples taken and iv been told my iron saturation is low, can anybody explain this to me and would it be contributing to my rls which is crazy...
Prevagen has been touted as a dietary supplement that helps to improve memory. Does Prevagen work?. Prevagen is a dietary supplement made by Quincy Bioscience, a company based in Wisconsin. It contains apoaequorin, a protein derived from a jellyfish. Evidence cited by Quincy Bioscience that Prevagen is effective is reported in a study in 2016. This study was not published in any journal.. The goal of the study was to determine whether the active ingredient of Prevagen, apoaequorin, improves cognitive function in older adults who have normal or near normal memory function. In this study, healthy adults ages 40-91 with memory concerns were examined by cognitive tests over a period of 90 days. People with neurological diseases and other conditions were excluded from the study population.. The authors reported that there were significant improvements in cognitive function in people treated with the study chemical compared to those who were not.. Limitations of this study include:. The study duration ...
SABUN TEMULAWAK TIMBUL | WIDYA ORIGINAL HOLO HOLO BERBEDA2 SESUAI STOCK DARI SUPPLIER menghilangkan bintik hitam, jerawat dan kisut kisut pada kulit. kulit yang kasar dan hitam dapat berubah menjadi putih, bersih
In this study we show that the rhoptry-derived protein ROP2, the founding member of a family of rhoptry proteins exposed to the host cell cytosol (Beckers et al., 1994), mediates PVM-organelle association. This is achieved by the host cytoplasm-exposed domain, ROP2hc, inserting into organelle membranes and establishing a stable association. Despite possessing an NH2-terminal signal (Fig. 3 A; Beckers et al., 1994) with features on a matrix targeting signal (Neupert, 1997), ROP2hc insertion and translocation into the MOM (Fig. 3) does not occur by the conventional import pathway (Fig. 4). By what alternative mechanism is ROP2hc translocated across the MOM? ROP2hc import, presumably exposing its NH2 terminus to the intermembrane space (IMS), has features reminiscent of apocytochrome c import (Stuart and Neupert, 1990; Jordi et al., 1992; Dumont, 1996). ROP2hc shares some potentially important physical features with the IMS-localized cytochrome c and its receptor cytochrome c heme lyase (CCHL) ...
Safety assessment of Apoaequorin, a protein preparation: subchronic toxicity study in rats. - Daniel L Moran, Palma Ann Marone, Mark R Bauter, Madhu G Soni
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Prevagen has been touted as a dietary supplement that helps to improve memory. Does Prevagen work?. Prevagen is a dietary supplement made by Quincy Bioscience, a company based in Wisconsin. It contains apoaequorin, a protein derived from a jellyfish. Evidence cited by Quincy Bioscience that Prevagen is effective is reported in a study in 2016. This study was not published in any journal.. The goal of the study was to determine whether the active ingredient of Prevagen, apoaequorin, improves cognitive function in older adults who have normal or near normal memory function. In this study, healthy adults ages 40-91 with memory concerns were examined by cognitive tests over a period of 90 days. People with neurological diseases and other conditions were excluded from the study population.. The authors reported that there were significant improvements in cognitive function in people treated with the study chemical compared to those who were not.. Limitations of this study include:. The study duration ...
1LKJ: The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property.
AequoScreen parental cells stably expressing the mitochondrially targeted apoaequorin and the G-protein Ga16 for flash-luminescence assay. Recombinant, in CHO-K1 host cell. GPCRs of your choice can be transiently / stably transfected into this cell line. Following GPCR stimulation, increases in intracellular calcium enable measurement of the resulting flash luminescence signal. Two vials of cryopreserved cells are shipped per order. Terms and conditions apply. Please inquire at your local sales office for more information.. ...
1) Enzyme repression is the mode by which the synthesis of an enzyme is prevented by repressor molecules. In many cases, the end product of a synthesis chain (e.g., an amino acid) acts as a feed-back corepressor by combining with an intracellular aporepressor protein, so that this complex is able to block the function of an operator. As a result, the whole operation is prevented from being transcribed into mRNA, and the expression of all enzymes necessary for the synthesis of the end product enzyme is abolished.. ...
The appeal that Prevagen is making to consumers is a very old one: basically, they want you to think that if a protein is used in your brain, then eating that protein will make your brain healthier (even though apoaequorin is not a human protein). By this argument, I could package up hundreds of different proteins (perhaps thousands-the brain is a complex organ) and sell them as "brain food" This simplistic principle has been used for centuries in folk medicine: its the reason why some people think that eating the body parts of bears and tigers will make them more virile. But eating tiger organs doesnt make you more like a tiger. Its a form of magical thinking, and theres simply no science to support it. In short, its just wrong ...
The appeal that Prevagen is making to consumers is a very old one: basically, they want you to think that if a protein is used in your brain, then eating that protein will make your brain healthier (even though apoaequorin is not a human protein). By this argument, I could package up hundreds of different proteins (perhaps thousands-the brain is a complex organ) and sell them as "brain food" This simplistic principle has been used for centuries in folk medicine: its the reason why some people think that eating the body parts of bears and tigers will make them more virile. But eating tiger organs doesnt make you more like a tiger. Its a form of magical thinking, and theres simply no science to support it. In short, its just wrong ...
If you noticed the symptoms of illness in your dog, then never wait for regular check-ups. You should immediately visit your trusted veterinarian to find out the exact problem and the treatment of that problem. Regular Check-ups will assist in giving the vaccinations against rabies virus, corona virus, parvovirus, canine distemper, hepatitis virus, and many more.. During regular check-ups, the booster vaccinations will often be carried out immediately without delaying as it assists to enhance the dogs immunity power against the severe diseases. Check-ups in regular basis are the necessary ones with the proper examination of stools. Thus, the de-worming can also be carried out with the drug such as albendazole, fenbendazole, etc.. It is possible to remove the abnormalities such as signs of pain throughout such check-ups. If the regular check-ups are not conducted then your dog can be affected by the helminthiasis and it may result in loose motion and other several digestive upsets and anemia as ...
1. According to the Fletcher-Huehns hypothesis there exists a functional difference between the two iron-binding sites of transferrin.. 2. The aim of the study presented was to evaluate this hypothesis in a homogeneous system, with human bone marrow cells and pure human monoferric transferrins A and B.. 3. For this reason normal human bone marrow cells were incubated with human monoferric transferrin. The monoferric transferrins A and B were obtained by selective labelling at different pH of apotransferrin followed by preparative isoelectric focusing in granulated gels. The uptake of iron by the cell suspensions from monoferric transferrins A and B was equal.. 4. In a heterogeneous but more active system for the removal of iron from human transferrin in vitro the two human monoferric transferrins did not show any significant functional differences.. 5. No support for the Fletcher-Huehns hypothesis could be obtained. ...
Aequorin is a protein that contains coelenterazine as a luminescent compound and can be used for intracellular calcium ion detection. When three Ca2+ ions bind to the aequorin complex consisting of the 22 KD apoaequorin protein (APO), molecular oxygen and the luminophore coelenterazine, the latter is oxidized to coelenteramide with a concomitant release of CO2 and blue light. Since the intensity of bioluminescence emitted by aequorin upon calcium binding correlates with the Ca2+ concentration, a sensitive measurement of Ca2+ concentrations with a broad detection range (~0.1 µM to ,100 µM) is possible. Unlike fluorescent Ca2+ indicators, Ca2+-bound aequorin can be detected without illuminating the sample, thereby eliminating interference from autofluorescence ...
Complete information for HCCS gene (Protein Coding), Holocytochrome C Synthase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
... 3.65 (p,0.001) for 16, 24, and 32 weeks, respectively, compared to the 0 weeks
The interstitial lung diseases of childhood, so called chILD, until fairly recently were classified based upon histologic appearance and clinical outcomes and although these metrics are still useful; identification of the genetic causes of many of these diseases is making classification more precise and helping to identify potential therapeutic targets. Moreover, in the case of surfactant metabolism disorders of the neonate and infant, what were once considered histologically distinctly disorders, e.g. pulmonary alveolar proteinosis (PAP), nonspecific interstitial pneumonitis, diffuse interstitial pneumonitis, and chronic pneumonitis of infancy are now recognized to have related underlying genetic mechanisms making it possible to identify some patients with these disorders by genetic testing rather than by lung biopsy [8].. Using PAP as an example, it is now recognized that the severe, neonatal form is caused by deficiency in the hydrophobic surfactant apoprotein (Sp)B. Abnormalities in the ...
Preparation of CYP3A4 Apo-Protein. Removal of the heme from CYP3A4 and preparation of the apo-protein was performed by treatment with H2O2 (Uvarov et al., 1990; Pikuleva et al., 1992). We implemented very mild conditions of treatment to prevent any peroxidative damage of the protein. In brief, CYP3A4 was diluted to 50 μM in 100 mM sodium phosphate buffer, pH 7.2, 20% glycerol (buffer A). Catalase was added directly to this solution to a final concentration of 1.7 units/ml. The sample was then dialyzed in a Spectra/Por Type I molecular weight cut-off 6000-8000, 10-cm flat width dialysis bag (Spectrum Laboratories, Rancho Dominguez, CA) against 50 volumes of buffer A containing 100 mM H2O2. Dialysis was performed at 4°C with continuous stirring for 24 h. The sample was removed and was further dialyzed against 50 volumes of 100 mM 4-morpholinepropanesulfonic acid, pH 7.4, 10% glycerol, 1 mM EDTA, 0.2 mM dithiothreitol. Protein concentration was determined using the Bradford protein assay kit ...
Natures Way : Alive! (Iron-Free) - 60 Tabs - Affordable Natural Supplements. Vitamins, minerals, herbals, supplements, and natural products. Free shipping on orders over $100!
An increased plasma transferrin level is often seen in patients suffering from iron deficiency anemia, during pregnancy, and with the use of oral contraceptives, reflecting an increase in transferrin protein expression. When plasma transferrin levels rise, there is a reciprocal decrease in percent transferrin iron saturation, and a corresponding increase in total iron binding capacity in iron deficient states[14] A decreased plasma transferrin can occur in iron overload diseases and protein malnutrition. An absence of transferrin results from a rare genetic disorder known as atransferrinemia, a condition characterized by anemia and hemosiderosis in the heart and liver that leads to heart failure and many other complications. Transferrin and its receptor have been shown to diminish tumour cells when the receptor is used to attract antibodies.[9] ...
In molecular genetics, a repressor is a DNA- or RNA-binding protein that inhibits the expression of one or more genes by binding to the operator or associated silencers. A DNA-binding repressor blocks the attachment of RNA polymerase to the promoter, thus preventing transcription of the genes into messenger RNA. An RNA-binding repressor binds to the mRNA and prevents translation of the mRNA into protein. This blocking of expression is called repression. If an inducer, a molecule that initiates the gene expression, is present, then it can interact with the repressor protein and detach it from the operator. RNA polymerase then can transcribe the message (expressing the gene). A corepressor is a molecule that can bind to repressor and make it bind to the operator tightly, which decreases transcription. A repressor that binds with a corepressor is termed an aporepressor or inactive repressor. One type of aporepressor is the trp repressor, an important metabolic protein in bacteria. The above ...
The differentiation of myelin-forming Schwann cells (SC) is completed with the appearance of myelin proteins MBP and P(0) and a concomitant downregulation of markers GFAP and p75NTR, which are expressed by immature and adult non-myelin-forming SC. We have previously demonstrated that holotransferrin (hTf) can prevent SC dedifferentiation in culture (Salis et al., 2002), while apotransferrin (aTf) cannot. As a consequence, we used pure cultured SC and submitted them to serum deprivation in order to promote dedifferentiation and evaluate the prodifferentiating ability of ferric ammonium citrate (FAC) through the expression of MBP, P(0), p75NTR and c-myc. The levels of cAMP, CREB and p-CREB were also measured ...
The protein encoded by this gene is an enzyme that covalently links a heme group to the apoprotein of cytochrome c. Defects in this gene are a cause of microphthalmia syndromic type 7 (MCOPS7). Three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jan 2010 ...
|strong|Sheep anti Human transferrin antibody|/strong| recognizes human transferrin, also known as beta-1 metal-binding globulin siderophilin or serotransferrin. Transferrin is 647 amino acid ~7…
This is one of the new holo multichromes by I Love Nail Polish. Its got a blue-indigo-purple-red-gold shift which is just amazing. The holo adds a nice sparkle just at the colour shift in low light and is intensively, well, holographic in all colours in full light. The colour shift is so noticeable that even…
Acpp - Acpp (untagged ORF) - Rat acid phosphatase, prostate (Acpp), transcript variant 1, (10 ug) available for purchase from OriGene - Your Gene Company.
When not bound to iron, transferrin is known as "apotransferrin" (see also apoprotein). ...
1985). "AIMilano apoprotein identification of the complete kindred and evidence of a dominant genetic transmission". Am. J. Hum ... Franceschini G, Sirtori CR, Capurso A, Weisgraber KH, Mahley RW (1980). "A-IMilano apoprotein. Decreased high density ...
Apo B is an integral apoprotein whereas the others are peripheral apoproteins. Apolipoprotein L Saito H, Lund-Katz S, Phillips ...
The chromophore is unreactive when bound to the apoprotein. Upon its release, it reacts to form 1,4-didehydrobenzene and ... Chromoprotein enediynes are characterized by an unstable chromophore enediyne bound to an apoprotein. ...
... apoproteins, blood lipid levels, and tissue fatty acid composition in humans". Lipids. 32 (4): 427-33. doi:10.1007/s11745-997- ...
The lipoprotein particles have hydrophilic groups of phospholipids, cholesterol, and apoproteins directed outward. Such ... shielded from the water by the phospholipid monolayer and the apoproteins. The interaction of the proteins forming the surface ...
"Isolation and characterization of the human pulmonary surfactant apoprotein gene". Nature. 317 (6035): 361-3. doi:10.1038/ ...
Apoprotein-B inhibitor mipomersen (approved by the FDA in 2013 homozygous familial hypercholesterolemia.[7][8]). ...
There is a general decrease in the expression of apoproteins after C. oncophora infection. However, the resistant host still ... maintains higher level of apoproteins compared to low responder. There is a disruption of lipid metabolism. It is known that ...
... s also synthesize apoproteins with which they then assemble and export lipoproteins (VLDL, HDL). The liver is also ...
Rees, A; Shoulders, CC; Stocks, J; Galton, DJ; Baralle, FE (1983). "DNA polymorphism adjacent to human apoprotein A1 gene: ...
Significant interindividual variability in CYP2A6 apoprotein and mRNA levels has been observed. CYP2A6 is known to be inducible ...
... are the chromophores that bind through a covalent thioether bond to their apoproteins at cysteins residues. The apoprotein with ...
Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An enzyme together with the ... A Holoprotein or conjugated protein is an apoprotein combined with its prosthetic group. Some enzymes do not need additional ...
"Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein". Biochemistry. 21 (14): 3298- ...
Primary hyperlipoproteinemia Familial hypertriglyceridemia Lipoprotein lipase deficiency Familial apoprotein CII deficiency ...
Hills, BA (1994). "Release of surfactant and a myelin proteolipid apoprotein in spinal tissue by decompression". Undersea and ...
Reiser S, Powell AS, Scholfield DJ, Panda P, Ellwood KC, Canary JJ (May 1989). "Blood lipids, lipoproteins, apoproteins, and ...
February 1987). "Malabsorption, hypocholesterolemia, and fat-filled enterocytes with increased intestinal apoprotein B. ...
... at which point breakdown of the apoprotein occurs. An important enzyme in the breakdown of the apoprotein is FtsH6, which ... It is located in the thylakoid membrane of the chloroplast and it is composed of an apoprotein along with several ligands, the ...
Primary hyperlipoproteinemia Familial apoprotein CII deficiency List of cutaneous conditions Santamarina-Fojo, S (1998). " ...
Nabika T, Nasreen S, Kobayashi S, Masuda J (December 2002). "The genetic effect of the apoprotein AV gene on the serum ...
... which interacts with the apoprotein to ensure specific Fe-S cluster insertion.[47][48] ...
Weisgraber KH, Innerarity TL, Mahley RW (Mar 1982). "Abnormal lipoprotein receptor-binding activity of the human E apoprotein ...
The phytochrome apoprotein, a protein that together with a prosthetic group forms a particular biochemical molecule such as a ... Upon binding the chromophore, the holoprotein, an apoprotein combined with its prosthetic group, becomes sensitive to light. If ...
Brown WV, Baginsky ML: Inhibition of lipoprotein lipase by an apoprotein of human very low density lipoprotein. Biochem Biophys ...
Apoprotein may refer to: Apoenzyme, the protein part of an enzyme without its characteristic prosthetic group Apolipoprotein, a ...
Nutrition · Apoprotein · Cytochrome P450 · Cytochrome p450 2a6 · Cytochrome P450 2B6 · Cytochrome P450 2C19 · Cytochrome p450 ... The relative apoprotein levels of 11 CYP enzymes were determined using a panel of antipeptide antibodes. In addition, 7- ... PB and RIF increased the levels of CYP3A apoprotein and mRNA, whereas BNF down-regulated CYP3A and related activities. PB and ... Biology · Biotechnology · 4 hydroxy cinnamic acid · apoprotein · cinnamic acid derivative · coumaric acid · cysteine · glycine ...
Spontaneous activity of opsin apoprotein is a cause of Leber congenital amaurosis.. Woodruff ML1, Wang Z, Chung HY, Redmond TM ...
1993) N-3 fatty acids stimulate intracellular degradation of apoprotein B in rat hepatocytes. J Clin Invest 91:1380-1389.. ... Presecretory oxidation, aggregation, and autophagic destruction of apoprotein-B: A pathway for late-stage quality control. ... Presecretory oxidation, aggregation, and autophagic destruction of apoprotein-B: A pathway for late-stage quality control ... Presecretory oxidation, aggregation, and autophagic destruction of apoprotein-B: A pathway for late-stage quality control ...
Lipids, apoprotein B, and associated coronary risk factors in urban and rural older Mexican populations.. Aguilar-Salinas CA1, ...
... the MBR mutant apoproteins exhibited H/D exchange kinetics similar to the WT apoprotein, as did some of the more stable WT-like ... similar to or higher than that of the WT apoprotein (Tm = 52.5 degrees C). The apoproteins with substitutions remote from the ... whereas the less stable apoproteins exhibited significantly less protection from H/D exchange than the WT apoprotein. Most ... The results of H/D exchange compared with those of DSC for 12 ALS mutant SOD1S-S apoproteins. TMs as determined by DSC are ...
... seedlings by density labeling of apoprotein and radioactive labeling of heme moieties. The heavy isotope (50% (2)H(2)O) and the ... The turnover of catalase apoprotein and catalase heme was studied in cotyledons of sunflower (Helianthus annuus L.) ... Only small amounts of heme groups were recycled into newly synthesized apoprotein during growth in the light, and no evidence ... A degradation constant for catalase apoprotein of 0.263 per day was determined from the data on heme recycling and the ...
By use of lipoxygenase-oxidized 2-[1-14C]linoleoyl PtdCho as the substrate and delipidated apoprotein B (apo-B), evidence is ... Phospholipase A2 activity of low density lipoprotein: evidence for an intrinsic phospholipase A2 activity of apoprotein B-100. ... Phospholipase A2 activity of low density lipoprotein: evidence for an intrinsic phospholipase A2 activity of apoprotein B-100 ... Phospholipase A2 activity of low density lipoprotein: evidence for an intrinsic phospholipase A2 activity of apoprotein B-100 ...
Photosystem I P700 chlorophyll a apoprotein A1UniRule annotation. ,p>Manual validated information which has been generated by ... sp,A0T0M8,PSAA_THAPS Photosystem I P700 chlorophyll a apoprotein A1 OS=Thalassiosira pseudonana OX=35128 GN=psaA PE=3 SV=1 ...
Plasma Lipoprotein Subclasses and Apoproteins as Predictors of Coronary Atherosclerosis in Man F. Hammett; F. Hammett ... F. Hammett, S. Saltissi, S. Rao, N. Miller, J. Coltart, B. Lewis; Plasma Lipoprotein Subclasses and Apoproteins as Predictors ... Inter-relationships between small, dense low-density lipoprotein (LDL), plasma triacylglycerol and LDL apoprotein B in an ... Plasma High-Density Lipoprotein Metabolism in Subjects with Primary Hypertriglyceridaemia: Altered Metabolism of Apoproteins AI ...
Crystal structure of Staphylococcal nuclease variant Delta+PHS M98G apo protein at cryogenic temperature. ...
Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids. ... THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED ...
... intermittent administration of growth hormone to hypophysectomized female rats on serum lipoproteins and their apoproteins. ...
The proteorhodopsin apoprotein and the retinal analog form a photochromic material having different spectral properties from ... those of a corresponding photochromic material formed by the same proteorhodopsin apoprotein and all-trans-retinal. In one ... The present invention relates to a photochromic material comprising a proteorhodopsin apoprotein and a retinal analog. In one ... Proteorhodopsin apoprotein binds all-trans-retinal at a conserved lysine residue (K231 in Bac31A8 and K234 in Hot75M1) by a ...
... and apoproteins AII and E were unchanged during the HCLFD. Lipoprotein and apoprotein concentrations were independent of ... The effect of high carbohydrate, low fat diets on lipoprotein lipids, apoproteins, nutritional status and diabetic control in ... lipoprotein and apoprotein concentrations and nutritional status in IDDM. Six women with IDDM were studied in the Clinical ...
Human Apoprotein apo ELISA Kit is available 2 times from supplier bioassay at Gentaur.com shop ... Human Apoprotein apo ELISA Kit is available 2 times from Bioassay labs E3607Hu , Human Apoprotein A(APO-A)ELISA Kit size: 96T ... Short name Apoprotein A(APO-A)ELISA Kit Alternative name H. sapiens Apoprotein A(APO-A)Enzyme-linked immunosorbent assay ... E1428Hu , Human Apoprotein A4,apo-A4 ELISA Kit size: 96T , 726.55 USD ...
Relationship between Apoprotein AI and AII Kinetics and the Metabolism of Triglyceride-Rich Lipoproteins in Man S. N. Rao; S. N ... The role of apoproteins AI and AII in binding of high-density lipoprotein 3 to membranes derived from bovine aortic endothelial ... S. N. Rao, P. Magill, A. Nicoll, N. Miller, B. Lewis; Relationship between Apoprotein AI and AII Kinetics and the Metabolism of ... Plasma High-Density Lipoprotein Metabolism in Subjects with Primary Hypertriglyceridaemia: Altered Metabolism of Apoproteins AI ...
The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation Koslover, Daniel J ; ... Home , The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation ...
... and apoprotein A-I levels in hypercholesterolemic women and men after 1 year: the beFIT Study ... The effect of a high cholesterol and saturated fat diet on serum high-density lipoprotein-cholesterol, apoprotein A-I, and ... and apoprotein A-I levels in hypercholesterolemic women and men after 1 year: the beFIT Study. Walden, C.E.; Retzlaff, B.M.; ... and apoprotein A-I levels in hypercholesterolemic women and men after 1 year: the beFIT Study. ...
APO protein 1. APO protein 1 ELISA Kit. APO protein 1 Recombinant. APO protein 1 Antibody ... APO protein 2. APO protein 2 ELISA Kit. APO protein 2 Recombinant. APO protein 2 Antibody ... APO protein 3. APO protein 3 ELISA Kit. APO protein 3 Recombinant. APO protein 3 Antibody ... APO protein 4. APO protein 4 ELISA Kit. APO protein 4 Recombinant. APO protein 4 Antibody ...
APO2 recombinant protein :: APO protein 2, chloroplastic (APO2) Recombinant Protein. Catalog #. MBS1483648 ...
... pyrene-induced rise in rat liverCYP1A1 mRNA in a dose-dependent manner as well as the apoprotein levels of CYP1A. Conclusions: ... pyreneinducedrise in rat liver CYP1A1 mRNA and apoprotein levels. Materials and Methods: Precision cut rat liverslices were ... followedby determination of CYP1A1 mRNA and apoprotein levels using quantitative polymerase chain reaction andimmunoblotting. ... "Inhibitory effect of Phenethyl Isothiocyanate Against Benzo[a] Pyrene-Induced Rise in CYP1A1 mRNA and Apoprotein Levels as its ...
Apoproteins Despite the fact that apoC-III does not bind biglycan directly, recent data showed that the apoC-III content of ... This is thought to primarily involve the interactions of apoproteins with proteoglycans or other matrix molecules. ...
Jue, T., Krishnamoorthi, R., & La Mar, G. N. (1983). Proton NMR study of the mechanism of the heme-apoprotein reaction for ... Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin. / Jue, Thomas; Krishnamoorthi, R.; La Mar, ... Jue, T, Krishnamoorthi, R & La Mar, GN 1983, Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin ... Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin. Journal of the American Chemical Society. 1983 ...
  • Thus, the ALS mutant Cu,Zn-superoxide dismutase apoproteins do not all share reduced global stability, and additional properties must be identified and understood to explain the toxicity of all of the mutant proteins. (nih.gov)
  • An important enzyme in the breakdown of the apoprotein is FtsH6, which belongs to the FtsH family of proteases. (wikipedia.org)
  • This enzyme catalyses the following chemical reaction (1) ATP + lipoate ⇌ {\displaystyle \rightleftharpoons } diphosphate + lipoyl-AMP (2) lipoyl-AMP + apoprotein ⇌ {\displaystyle \rightleftharpoons } protein N6-(lipoyl)lysine + AMP This enzyme requires Mg2+ as a cofactor. (wikipedia.org)
  • They also serve as carriers for molecules of low water solubility this way isolating their hydrophobic nature, including lipid-soluble hormones, bile salts, unconjugated bilirubin, free fatty acids (apoprotein), calcium, ions (transferrin), and some drugs like warfarin, phenobutazone, clofibrate & phenytoin. (wikipedia.org)
  • The pigments, such as phycocyanobilin and phycoerythrobilin, are the chromophores that bind through a covalent thioether bond to their apoproteins at cysteins residues. (wikipedia.org)
  • A study found that the acclimative modulation of PSII antenna size only involves the outer light harvesting complexes of PSII (LHC-PSII) caused by the proteolysis of its apoprotein. (wikipedia.org)
  • Dixon published a series of papers on D-amino acid oxidase, detailing the kinetics and thermodynamics of association of the coenzyme with the apoprotein, the substrate and inhibitor specificity, and the effect of pH on the kinetic constants. (wikipedia.org)
  • E2 binding to the apoprotein of native LDL, through a specific and saturable receptor, inhibits misfolding phenomenon despite an unaffected production of LDL (-) by phospholipase A2, ultimately preventing LDL aggregation. (eurekaselect.com)
  • Most striking were the three mutant apoproteins, D101N, E100K, and N139K, which have apparently normal metallation properties, and differ little from the WT apoprotein in either thermal stability or H/D exchange kinetics. (nih.gov)
  • In 1997, en route to the originally reported structure, researchers under the direction of Masahiro Hirama discovered that the spectroscopic data of the proposed chloroazatyrosyl (S)-α-amino acid derivative were not consistent with those of the degradation product characterized by Leet et al. (wikipedia.org)
  • Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. (wikipedia.org)
  • Both patterns contain conserved histidine, tryptophan and acidic residues which could be important for the interaction of the enzymes with the apoproteins and/or the haem group. (wikipedia.org)
  • The relative stabilities and structural properties of a representative set of 20 ALS-mutant Cu,Zn-superoxide dismutase apoproteins were examined by using differential scanning calorimetry and hydrogen-deuterium (H/D) exchange followed by MS. Contrary to recent reports from other laboratories, we found that ALS-mutant apoproteins are not universally destabilized by the disease-causing mutations. (nih.gov)