Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes of proteinase-inhibitory system values in blood plasma of dogs with experimental acute pancreatitis (EAP) were studied in dynamics. Their diagnostic and prognostic values was appraised. Essential shifts were revealed in the proteinase-inhibitory balance in blood plasma of dogs with EAP of various severity. The concentration of trypsin- and chymotrypsin-like proteinases exceeded the normal values 1.8-3.3 times in these animals. Coefficients expressing the relation of antitryptic and antichymotryptic activities to the activities of the corresponding proteinases in the blood plasma of animals with EAP were indicative of diminished blood plasma inhibitory potential as compared to that in intact animals. The authors are the first to show the diagnostic and prognostic value of the antichymotryptic activity/chymotrypsin in blood plasma of dogs with EAP.
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PMID:[Dynamics of changes in the protease-inhibitory balance in blood plasma of dogs with experimental acute pancreatitis]. 205 39

Proteases released by larvae of the sheep blowfly have been suggested to have a primary role in wound formation and larval nutrition. Assays were carried out on two larval products to analyse the substrate specificity of these proteases, their abundance and approximate molecular weights. Tryptic and chymotryptic activities were found in both products though there were more chymotrypsin-like enzymes in products from 48 h cultures (CESP) than in product collected direct from 48 h larvae (LESP). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels incubated with azocasein showed plaques of major enzyme activity at molecular weights of 20,000 and 26,000 in LESP and at 20,000 in CESP, SDS-PAGE gels, when reacted with peptide substrates showed tryptic activity at 20,000 and 26,000 in LESP, whereas CESP showed only chymotryptic activity at 20,000 and higher molecular weights. The results suggest at least three enzymes, a trypsin and chymotrypsin in LESP, a chymotrypsin in CESP and a tryptic enzyme which is not stable to SDS-PAGE probably in both LESP and CESP. In addition, reactivity with elastase and plasmin substrates suggests the presence of enzymes with general effects on skin substrates and inflammatory pathways.
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PMID:Tryptic and chymotryptic proteases released by larvae of the blowfly, Lucilia cuprina. 207 26

Results of the comparative study of trypsin- and chymotrypsin-like serine proteases from pyloric caeca of salmon fishes and trypsin and chymotrypsin of bulls are presented in the paper. The hydrolytic activity of salmon proteases with respect to methyl ethers of N-benzoyl-L-leucine is 2.4 times higher than that of bull chymotrypsin, but with respect to methyl esters of N-benzoyl-L-tyrosine and N-benzoyl-L-arginine the activity of salmon proteases is 6.5 and 80 times lower than that of bull chymotrypsin and trypsin. Salmon proteases in contrast to bull trypsin and chymotrypsin hydrolyze but slightly N-glutaryl-L-phenylalanine para-nitroanilide. It shown that fish proteases are not absolutely specific to synthetic substrates, which is a result of their less pronounced (than in case of bull trypsin and chymotrypsin) differences in structures of binding centres. The study of the salmon protease interaction with some immobilized ligands has confirmed the higher affinity of enzymes to reagents with two space-separated aromatic rings in their composition. It is supposed that salmon proteases interact with such reagents through two sites: hydrophobic "pockets" and probably additional binding site of the active centre. The salmon protease preparation demonstrates higher resistance to inactivating action of formaldehyde within the range of concentrations 2-16% than bull chymotrypsin does.
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PMID:[Comparative study of the properties of serine proteases of lower and higher vertebrates]. 208 90

Multicatalytic proteinase (MCP) was solubilized from human erythrocyte membrane with 0.1% Triton X-100 and purified to homogeneity using a combination of DEAE-cellulose, hydroxylapatite, and Ultrogel AcA34 chromatographies. This membranous MCP had similar properties to MCP purified in parallel from the cytosol. Both MCPs had a molecular mass of 570 kDa, were composed of apparently nine subunits of 22-36 kDa and had trypsin- and chymotrypsin-like activities. These activities were latent and required heating for the induction. However, slight differences were observed in the effects of reagents (DFP, monoiodoacetic acid, Mg2+, and Ca2+) between membranous and cytosolic MCP. The amount of MCP identified on membranes was estimated to be three-quarters or one-half of that found in the cytosol based on its trypsin- or chymotrypsin-like activity, respectively.
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PMID:Significant amount of multicatalytic proteinase identified on membrane from human erythrocyte. 218 58

Human mast cells can be divided into two subsets based on serine proteinase composition: a subset that contains the serine proteinases tryptase and chymase (MCTC), and a subset that contains only tryptase (MCT). In this study we examined both types of mast cells for two additional proteinases, cathepsin G and elastase, which are the major serine proteinases of neutrophils. Because human mast cell chymase and cathepsin G are both chymotrypsin-like proteinases, the properties of these enzymes were further defined to confirm their distinctiveness. Comparison of their N-terminal sequences showed 30% nonidentity over the first 35 amino acids, and comparison of their amino acid compositions demonstrated a marked difference in their Arg/Lys ratios, which was approximately 1 for chymase and 10 for cathepsin G. Endoglycosidase F treatment increased the electrophoretic mobility of chymase on SDS gels, indicating significant N-linked carbohydrate on chymase; no effect was observed on cathepsin G. Immunoprecipitation and immunoblotting with specific antisera to each proteinase revealed little, if any, detectable cross-reactivity. Immunocytochemical studies showed selective labelling of MCTC type mast cells by cathepsin G antiserum in sections of human skin, lung, and bowel. No labeling of mast cells by elastase antiserum was detected in the same tissues, or in dispersed mast cells from lung and skin. A protein cross-reactive with cathepsin G was identified in extracts of human skin mast cells by immunoblot analysis. This protein had a slightly higher Mr (30,000) than the predominant form of neutrophil cathepsin G (Mr 28,000), and could not be separated from chymase (Mr 30,000) by SDS gel electrophoresis because of the size similarity. Using casein, a protein substrate hydrolyzed at comparable rates by chymase and cathepsin G, it was shown that about 30% of the caseinolytic activity in mast cell extracts was sensitive to inhibitors of cathepsin G that had no effect on chymase. Hydrolytic activity characteristic of elastase was not detected in these extracts. These studies indicate that human MCTC mast cells may contain two different chymotrypsin-like proteinases: chymase and a proteinase more closely related to cathepsin G, both of which are undetectable in MCT mast cells. Neutrophil elastase, on the other hand, was not detected in human mast cells by our procedures.
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PMID:Identification of a cathepsin G-like proteinase in the MCTC type of human mast cell. 221 56

In Ciona intestinalis, sperm penetration through the egg vitelline coat is an essential event of fertilization. We investigated whether trypsin- and chymotrypsin-like enzymes are involved in this event. Inhibitors and peptide substrates for chymotrypsin-like enzymes blocked the overall process of fertilization in a concentration-dependent manner. The inhibitory activity was specifically exerted on the step of sperm penetration. Chymotrypsin-like protease activity was identified in spermatozoa with the fluorogenic synthetic substrate Suc-Ala-Ala-Phe-AMC, which was the most effective substrate in blocking sperm penetration. These data indicate that a chymotrypsin-like protease activity is a sperm lysin of Ciona intestinalis.
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PMID:Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coat of Ciona intestinalis egg. 222 80

Chicken liver multicatalytic proteinase is composed of multiple components with molecular masses ranging from 23 to 34 kDa and has 'chymotrypsin-like' and 'trypsin-like' activities, which were examined by using the chromogenic peptide substrates, succinyl-Phe-Leu-Phe-pNA(p-nitroanilide) and N-benzoyl-Phe-Val-Arg-pNA, respectively. Treatment of the enzyme with diisopropyl fluorophosphate (DFP) completely abolished the 'chymotrypsin-like' activity, but had little effect on the 'trypsin-like' activity. In the experiment with radio-labeled DFP, SDS-PAGE of the modified enzyme revealed that the radioactivity was incorporated into only the smallest subunit (23 kDa). The migration of this subunit was retarded on SDS-PAGE after the treatment with DFP.
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PMID:'Chymotrypsin-like' activity of chicken liver multicatalytic proteinase resides in the smallest subunit. 226 74

Data on alpha-chymotrypsin interactions with hydrophobic low-molecular compounds have been generalized. Existence of two sites of noncovalent interaction with hydrophobic nuclei of a ligand molecule is shown. When the substance to be bound contains only one hydrophobic nucleus, the interaction is mediated by a "hydrophobic pocket" of the enzyme--a binding site of amino acid residues which are, in the P1-position relative to the cleaved bond. Under these conditions substances with an asymmetric hydrophobic nucleus (of the tryptophan type) are better ligands for binding. In case of compounds containing several hydrophobic groups scattered in the space, interaction with the enzyme proceeds in two binding sites. New data are presented on the ligand specificity for binding sites of chymotrypsin in lower vertebrates. Relative position of hydrophobic groups of the ligand is shown as that of great importance for interaction with the enzyme. It is concluded that the binding sites of trypsin- and chymotrypsin-like proteinases of the lower vertebrates differ but less from each other as compared to binding sites of trypsin and chymotrypsin in mammals.
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PMID:[Hydrophobic interaction of alpha-chymotrypsin with low molecular weight compounds]. 227 Jun 21

We present here a detailed study of the effect of detergents on the three peptidase activities (hydrolysis of the LLVY, ARR, and LLE peptides) of the purified multicatalytic proteinase from rat liver. At Triton X-100 and sodium dodecyl sulfate (SDS) concentrations of 0.1%, all three peptidase activities are inhibited. Lower concentrations of the two detergents (0.01%) do not affect the hydrolysis of the ARR peptide, whereas they behave differently on the hydrolysis of the LLVY and LLE peptides. Triton X-100 inhibits and SDS strongly activates LLVY peptide hydrolysis by decreasing and increasing Vmax, respectively. In the absence of detergents, the saturation curve for the LLE peptide can be analyzed as the result of two components, one showing cooperative (nH = 1.6) with higher affinity (S0.5 = 60 microM) and lower Vmax than a second, noncooperative component (Km = 320 microM). SDS (0.01%) activates LLE peptide hydrolysis by suppressing cooperativity, slightly increasing Vmax, and decreasing the half-saturation concentration (Km = 30 microM) of the enzyme. Triton X-100 (0.01%) also suppresses the cooperativity and decreases the half-saturation concentration (Km = 25 microM) for the LLE peptide; in contrast, it reduces Vmax by inhibition of the low affinity, high Vmax component observed in the absence of detergents. Based on these observations, it can be concluded that both detergents behave like allosteric activators of peptidylglutamyl-peptide hydrolyzing activity and that the multicatalytic proteinase has at least three different classes of active sites: two independent noncooperative sites that catalyze the hydrolysis of trypsin and chymotrypsin-like substrates and one class for peptidylglutamyl-peptide hydrolysis having two components: one cooperative (two or more sites) and one noncooperative.
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PMID:Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver. 238 Jan 98

We have analyzed prostatic proteins of canine and human seminal plasma. We have compared in particular the physicochemical characteristics of arginine esterase from dog to those of the prostatic specific antigen from man. Both are major secretory proteins in each species. Arginine esterase and prostate specific antigen are related enzymes belonging to the serine-protease class. Their enzymatic activity towards protein substrates appears similar. However their activity towards synthetic substrates indicate that arginine esterase is a trypsin-like enzyme whereas prostate specific antigen has some chymotrypsin-like activity. The canine enzyme is inhibited by phenylmethylsulfonyl fluoride while the human one is not. The amino acid sequence of a portion of the NH2-terminal of the 2 proteins share 58% homology. Their molecular weights are similar: 29 KDa for arginine esterase and 34 KDa for prostate specific antigen. These results show that arginine esterase and prostate specific antigen are distinct but closely related proteins. These results strongly suggest that the dog could be an excellent model for the elucidation of the presently unknown role of this class of abundant enzymes of prostatic origin.
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PMID:Dog prostate arginine esterase is related to human prostate specific antigen. 242 May


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