Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

From mouse spinal cord homogenate, we isolated a trophic substance which reverses the post-denervation decrease in tetrodotoxin sensitivity of action potential in organ-cultured extensor digitorum longus muscle of mouse and characterized its physicochemical properties. The trophic substance was separated from macromolecules in homogenate by gel filtration on Biogel P2 column. The partially purified trophic substance was heat-stable, acid-stable and alkaline-labile. The trophic activity was destroyed by lyophilization at neutral pH but not at acidic pH. The trophic activity was abolished by incubation with pronase or leucine aminopeptidase, but not by trypsin, chymotrypsin, thermolysin or carboxypeptidase A. The trophic substance passed through an ultrafiltration membrane UM10 freely. A small part of the trophic activity passed through a UM2 or UM05, and the rest was retained on the membranes. The trophic substance adsorbed on CM-Sephadex at pH 7.2 but passed through DEAE-Sephadex at pH 8.4. These results suggest that the trophic substance regulating tetrodotoxin sensitivity of action potential in mouse skeletal muscle is a peptide with a rather low molecular weight of less than 10,000 and that while the N-terminus of the peptide is free, the C-terminus is probably blocked. This peptide differs from other trophic substances reported previously by other investigators.
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PMID:Partial purification and characterization of neutrophic substance affecting tetrodotoxin sensitivity of organ-cultured mouse muscle. 48 37

Effects of proteinase inhibitors on total proteolytic activity and trypsin and chymotrypsin activity in human pancreatic juice were determined separately. Purified inhibitors as well as crude extracts of raw soybeans completely inhibited trypsin and chymotrypsin activity while 40 to 50% of the total proteolytic activity remained. Inhibition experiments with 1,10-o-phenanthroline showed that this residual proteolytic activity was due mainly to carboxypeptidase A and B. Comparative studies with rat pancreatic enzymes demonstrated certain similarities between the corresponding enzymes from rat and man. However, differences were revealed which indicate that the rat enzymes must be used with great caution when applied as models for the human proteinases when studying effects of soybean inhibitors.
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PMID:Inhibition of human and rat pancreatic proteinases by crude and purified soybean proteinase inhibitors. 57 Oct 12

Properties of carboxypeptidase A of cultured skin fibroblasts from control and cystic fibrosis patients were studied using alpha-N-carbobenzoxy-L-glutamyl-L-tyrosine as substrate. Carboxypeptidase A was inhibited by thiomersal, cyanide, iodoacetate and N-ethylmaleimide in a similar manner for control and cystic fibrosis fibroblasts. Both trypsin and dithiothreitol treatment activated the enzyme, but 1,10-phenanthroline inhibited only in the presence of dithiothreitol. Both Zn2+ and Co2+ reversed this inhibition. Trypsin treatment of carboxypeptidase A produced a form of the enzyme having a higher KM value for both control and cystic fibrosis fibroblasts. Dithiothreitol treatment of control fibroblasts resulted in a form with similar properties to the trypsin activated form, but cystic fibrosis fibroblasts yielded a variant form with even higher KM and Vmax values. Since other properties were similar, it seems likely that this difference reflected binding of a molecule to the enzyme rather than of a defect in the enzyme.
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PMID:Carboxypeptidase A activity of cultured skin fibroblasts and relationship to cystic fibrosis. 66 47

The interaction of human plasma alpha-1-antichymotrypsin with serine proteinases from different tissues has been investigated. The protein was found to form stable complexes with pancreatic chymotrypsin, leukocyte cathepsin G, and mast cell chymotrypsin. No inhibition of pancreatic trypsin or leukocyte elastase could be demonstrated. With mixtures containing both alpha-1-antichymotrypsin and alpha-1-proteinase inhibitor, it was found that the former preferentially inactivated leukocyte cathepsin G, while the latter showed a strong preference for pancreatic chymotrypsin. However, leukocyte elastase was specifically inactivated by alpha-1-proteinase inhibitor even in 1:1 mixtures with chymotrypsin. All of these results taken together suggest that one of the primary functions of alpha-1-antichymotrypsin is to inactivate leukocyte cathepsin G, while alpha-1-proteinase inhibitor controls the activity of other serine proteinases, particularly leukocyte elastase.
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PMID:Human alpha-1-antichymotrypsin: interaction with chymotrypsin-like proteinases. 72 23

The various peptidases secreted by such exocrine tissues as gastric mucosa, pancreas and prostate are usually determined by catalytic methods. Another approach utilizes immunoassay. Endopeptidases were formerly assayed with protein substrates such as hemoglobin and albumin. These techniques are increasingly replaced by more specific ones using artificial peptide derivatives as substrates, some of which allow an increase in absorbance or fluorescence to be continuously recorded. The presently available methods of assaying pepsin, pancreatic trypsin, trypsinogen and carboxypeptidase A, enterokinase and several peptidases of human sperm are reviewed.
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PMID:The assay of exocrinous peptidases in clinical chemistry. 77 94

Lyophilized bovine, porcine, and human choroid plexuses contain .02-.09 U of antidiuretic activity per milligram. The antidiuretic factor in bovine choroid plexus was concentrated 100 times by extraction with acetic acid, fractional precipitation with acetone and ethyl ether, gel filtration, and paper chromatography. Resulting choroid plexus fraction IIgammaB2 was eluted from Sephadex G-25 in position corresponding to molecular weight between 750 and 3,500; its antidiuretic activity was destroyed by trypsin, performic acid, and thioglycollic acid, but was not affected by leucine aminopeptidase, carboxypeptidase A or B, or cyanogen bromide. HgammaB2 possesses antidiuretic, pressor, and oxytocic potencies (measured in anesthetized-hydrated rat, anesthetized rat, and isolated rat uterus, respectively) of 1.9, 0.5, and 0.1 U/mg, respectively.
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PMID:Antidiuretic peptide in mammalian choroid plexus. 81 22

The enzymic hydrolysis of some proteins (insulin-B-chain-S-sulfonate, S-aminoethylated lysozyme, bovine serum albumin) by immobilized peptidolytic enzymes is reported. Sepharose-bound pronase, trypsin and a protease from Thermoactinomyces sp. (MP), the latter both cross linked by glutaric dialdehyde and an exopeptidase mixture containing Sepharose-bound leucine aminopeptidase, carboxypeptidase A and a crude preparation of prolidase were used. After enzymic hydrolysis nearly all amino acids, except proline, were recovered in a 100% yield compared to the value of an acid reference hydrolysate. Tryptophan and methionine, which are partially destroyed by acid hydrolysis in the presence of oxygen could be recovered completely.
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PMID:[Protein hydrolysis by immobilized enzymes]. 98 21

1. D-Galactose dehydrogenase from Pseudomonas saccharophila (molecular weight 102 000) dissociates in 8 M urea into its subunits (molecular weight 25 000) which migrate in polyacrylamide gels, containing 8 M urea, as a single band. 2. The N-terminal residue determination by the dansyl method revealed only serine. 3. The C-terminal group determination with carboxypeptidase A and B indicated the sequence -Tyr-His-Leu. Leucine as the single C-terminal amino acid was confirmed by the tritiation method and by tritiation and subsequent degradation with carboxypeptidases. 4. The fragmentation of D-galactose dehydrogenase (24 mol methionine per mol enzyme) by CNBr resulted in six peptides, as detected in disc electrophoresis and substantiated by end group determination, indicating the identity of the subunits. 5. The treatment of D-galactose dehydrogenase (24 mol lysine and 52 mol arginine per mol enzyme) with trypsin and subsequent peptide mapping showed 21, perhaps 22 peptides, indicating a structure comprising four identical subunits.
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PMID:Subunit structure of D-galactose dehydrogenase from Pseudomonas saccharophila. 113 86

The seminal plasma and sperm of fresh and stored poultry semen were analyzed for the presence of eight peptide hydrolase enzymes. Five enzymes: carboxypeptidase A, carboxypeptidase B, chymotrypsin, glycylglycylglycine hydrolase and pepsin were not present in either plasma or sperm. An aminopeptidase-like and a cathepsin-like activity were found in seminal plasma and sperm while a trypsin-like activity was found in sperm only. There was a significant difference between full sib groups with respect to aminopeptidase-like activity in fresh and stored plasma, while storage for 24 hours resulted in a significant increase in trypsin-like activity of sperm. The aminopeptidase-like activity of fresh sperm was positively correlated with duration and percent fertility of fresh semen, while neither cathepsin-like activity nor trypsin-like activity were correlated with fertility of fresh or stored semen except for a positive correlation between the cathepsin-like activity of fresh plasma and percent fertility of fresh semen.
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PMID:The activity of some peptide hydrolase enzymes in fresh and stored poultry semen from full sib groups of males and their relationship to fertility. 118 12

The method of high-voltage paper electrophoresis may be applied not only for peptide separation, but also in modifications and combinations with other methods, so, by means of aminoethylation and maleylation it is possible to broaden or narrow the range of trypsin action. This, in its turn, makes it possible to isolate preparatively lysin- and arginine-containing peptides, oxidation with performic acid enables the thyol-containing fragments to be isolated and application of carboxypeptidase A-C-terminal peptide of protein. When studying the primary structure of proteins the method has already found its widest application but with an increase in the number of methods of protein specific modification its potentiabilities will be even wider.
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PMID:[High-voltage electrophoresis and its application in combination with other methods for protein structure studies]. 121 56


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