Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat vaginal epithelial cells have trypsin-like activity as shown by the formation of a colored product when the cells are incubated with alpha-N-methyl alpha-N-toxyl-L-lysine beta-naphthol ester and hexazotized pararosanilin. This enzyme activity in vaginal smears is maximal at proestrus, i.e., the day in the 5-day estrus cycle when plasma estrogen is maximal. Only the rounded nucleated epithelial cells present at late diestrus, proestrus and early estrus demonstrate the trypsin-like enzyme activity. These are the cells that stain blue in the Papanicolaou method. Preincubation of cell suspensions with the serine protease inhibitor, p-nitrophenyl p-guanidino benzoate, prevented the enzyme staining reaction, further demonstrating the trypsin-like nature of the cellular enzyme. The advantages of this enzyme staining technique over the fibrin plate method for the demonstration of trypsin-like enzymes in cells are increased resolution and ability to show trypsin inhibitor effects.
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PMID:Trypsin-like activity in the vaginal epithelial cells of the rat. 7

Clostridiopeptidase B (EC 3.4.22.8) was not inhibited by stoichiometric amounts of lima bean trypsin inhibitor, ovomucoid trypsin inhibitor, Kuntiz bovine trypsin inhibotor, Kunitz soybean trypsin inhibitor or ovoinhibitor. Activity was diminished at relatively high concentrations of the three latter inhibitors. Human plasma alpha 2-macroglobulin inhibited both the amidase and protease activity of the enzyme. Rat and dog plasmas contained high molecular weight inhibitors, presumably macroglobulins as well. Inhibition by this component was greater in rat plasma than in dog plasma, which may be related to the observation that clostridiopeptidase B-induced generation of kinin activity is indirect in the former plasma, but direct in the later. Leupeptin (N-acetyl-L-leucyl-L-leucyl-L-argininal) and antipain ([S)-1-carboxy-2-phenylethyl] carbamoyl-L-arginyl-L-valyl-L-argininal) inhibited clostridiopeptidase B (Ki of 2 . 10(-8) and 3 . 10(-8) M, respectively). They were potent inhibitors of clostridiopeptidase B-induced kinin release in dog plasma.
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PMID:Clostridiopeptidase B inhibition by plasma marcroglobulins and microbial antiproteases. 8 Feb 31

The effect of simultaneous intravenous administration in the dog of bovine trypsin and Trasylol followed by continued infusion of Trasylol was studied. Special attention was paid to the interchange between the dominating plasma protease inhibitors alpha1-antitrypsin and a-macroglobulins and to the disappearance of Trasylol and its trypsin complexes from the circulation. The following results were obtained: 1) Trypsin was preferentially bound by the alpha-macroglobulins, though Trasylol is a strong trypsin inhibitor. 2) On saturation of the alpha-macroglobulins, a considerable amount of trypsin was bound by alpha1-antitrypsin. 3) Trasylol was bound to the trypsin-alpha-macroglobulin complexes and then rapidly eliminated from the circulation. 4) On saturation of the alpha-macroglobulins, Trasylol was identified in a free form but increasing amounts of Trasylol were also bound to trypsin. This could be explained not only by direct complexation of Trasylol and trypsin but also by a transfer of trypsin from unstable trypsin-alpha1-antitrypsin complexes to free Trasylol.
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PMID:Trasylol prevents trypsin-induced shock in dogs. 8 67

The acid-stable trypsin inhibitor of human serum and urine is released in vivo by limited proteolysis from the high molecular weight, acid-labile inter-alpha-trypsin inhibitor. When complexed with trypsin, both this acid-stable, active derivative and the inter-alpha-trypsin inhibitor can be degraded in vitro by prolonged digestion with trypsin to a low molecular weight "minimal" inhibitor. This minimal trypsin inhibitor was sequenced and found to be homologous to the known Kunitz-type inhibitors (e.g. the basic trypsin-kallikrein inhibitor from bovine organs). This indicates that the antitryptic activity of the big inter-alpha-trypsin inhibitor is due to a Kunitz-type domain.
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PMID:Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, I. Determination of the amino acid sequence of the antitryptic domain by solid-phase Edman degradation. 9 47

40% of the primary structure of the cow colostrum proteinase inhibitor (CTI) is homologous with the structure of the trypsin kallikrein inhibitor (TKI) from bovine organs; the positions of the reactive lysine residues are also the same in both inhibitors. Both CTI and TKI were modified by carbamoylation and the fully labeled derivatives were isolated by ion-exchange chromatography. The effect of the modification on the antitryptic and antichymotryptic activity of both inhibitors was investigated. The antichymotryptic activity of both inhibitors is not decreased after the modification. The antitryptic activity of modified TKI is retained, yet the dissociation constant of the complex of the modified inhibitor with trypsin is considerably increased; nevertheless, modified TKI is a good trypsin inhibitor. The antitryptic activity of modified CTI is hardly detectable. We explain this difference in the behaviour of both inhibitors by a replacement of basic residues Arg-17 and Arg-39 in TKI by neutral amino acids Ala-20 and Gln-42 in CTI.
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PMID:Effect of modification of reactive lysine on antitryptic and antichymotryptic activity of proteinase inhibitor from cow colostrum. 9 62

Characterization of the trypsin-, chymotrypsin- and elastase-inhibiting properties of porcine serum was carried out by gel filtration on Ultrogel, AcA 44, and agarose gel electrophoresis with subsequent processing for protease-inhibiting activity. Moreover, by allowing the fractions obtained from gel filtration to react with antibodies to porcine serum protease inhibitors, the specific inhibiting properties of these inhibitor molecules were identified. At least six protease inhibitors were identified and partially characterized in porcine serum. Two alpha 2 -macroglobulins (alpha 2 Mf and alpha 2 Ms), homologues to human alpha 2 -macroglobulin, with slightly different electrophoretic mobilities, were both found to exhibit trypsin, chymotrypsin and elastase inhibiting activity. Alpha 1 -Protease inhibitor (Mr 51 000), a homologue to human alpha 1 -protease inhibitor (alpha 1 -antitrypsin), also showed trypsin-, chymotrypsin- and elastase-inhibiting properties. Inter-alpha-trypsin inhibitor (Mr 162 000 and 129000), a porcine serum counterpart to human inter-alpha-trypsin inhibitor, showed trypsin- and chymo-trypsin-inhibiting properties. In addition, a specific trypsin inhibitor, alpha 2 -antigrypsin (Mr 58 000), and a specific elastase inhibitor, beta-elastase inhibitor, were characterized in porcine serum, and these seem to have no counterparts in human serum.
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PMID:Identification and characterization of trypsin, chymotrypsin and elastase inhibitors in porcine serum. 9 64

The effect of intraduodenally administered trypsin on pancreatic exocrine secretion was investigated in conscious rats surgically prepared with bile--pancreatic fistulae. Introduction of NaHCO3 into the duodenum did not influence pancreatic secretion. Reintroduction of bile--pancreatic juice into the duodenum, however, suppressed pancreatic protein output, mainly because of changes in protein concentration. Infusion of trypsin into the duodenum in the absence of intraluminal pancreatic juice significantly suppressed the secretory volume and pancreatic enzyme output; addition of trypsin inhibitor to the trypsin infusion resulted in an immediate increase of pancreatic secretion. Trypsin inhibitor per se, however, was without effect. Bile--pancreatic juice affected amylase, kipase, and trypsinogen output in a parallel fashion; after addition of trypsin inhibitor to the infusion the inhibitory effects on pancreatic enzyme output was reversed in a parallel manner. The results support the hypothesis that pancreatic exocrine secretion is regulated by a feedback mechanism exerted--at least partly--by intraluminal trypsin.
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PMID:Trypsin as a regulator of pancreatic secretion in the rat. 9 75

1. Bovine (Bos taurus) trypsin and trypsin activity in rat (Rattus norvegicus) pancreatic extract were inhibited by soybean trypsin inhibitor and by bovine basic pancreatic and colostrum inhibitors. 2. Bovine alpha-chymotrypsin was inhibited by soybean and bovine basic pancreatic inhibitors but only weakly by colostrum inhibitor. 3. Chymotrypsin activity in rat pancreatic extract was due to at least three different components against all of which the inhibitors were largely ineffective. 4. It is concluded that bovine colostrum inhibitor has a more limited inhibition spectrum than the phylogenetically related basic pancreatic inhibitor which, in turn, is less active against rat than against bovine enzymes.
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PMID:Inhibition of rat and bovine trypsins and chymotrypsins by soybean, bovine basic pancreatic, and bovine colostrum trypsin inhibitors. 9 86

The trypsin inhibitor of bovine colostrum was isolated by affinity chromatography, and impurities removed by trichloroacetic acid precipitation. The inhibitor showed electrophoretic microheterogeneity which was not due to sialic acid content. It inhibited bovine and rat trypsin, showed weak inhibition of bovine chymotrypsin and was inactive against rat chymotrypsin and bovine renin, kallikrein, thrombin and trypsinogen. The dynamics of secretion of the inhibitor in the first 8 milkings post-partum were very similar to those of colostral immunoglobulins.
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PMID:Isolation and properties of bovine colostral trypsin inhibitor. 10 61

Glutamate decarboxylase, gamma-aminobutyrate-alpha-ketoglutarate aminotransferase and NAD-linked and NADP-linked succinic semialdehyde dehydrogenase, all constituting the GABA (gamma-aminobutyrate)-shunt pathway of glutamate metabolism are localized in the mitochondrial matrix in a streptomycin-bleached mutant of Euglena gracilis strain Z. Glutamate dehydrogenase, requiring NADP as the cofactor, was distributed in the cytoplasm. An improved version of the controlled digestion method for preparing Euglena mitochondria, which involves use of trypsin and a trypsin inhibitor and removal of broken cells before mechanical disruption of cells, is also described.
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PMID:Subcellular localization of the GABA-shunt enzymes in Euglena gracilis strain Z. 11 50


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