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)

From rat stomach, kallikrein was purified by chromatographies on columns of p-aminobenzamidine-Sepharose, DEAE-Sephadex A-50 and Sephadex G-150 and by isoelectric focusing, measuring its activities to hydrolyse prolylphenylalanyl-arginine-4-methyl-coumarine amide (Pro-Phe-Arg-MCA) and to release kinin from rat heated-plasma. The purified stomach kallikrein showed a single band on Disc electrophoresis at pH 7.0. The molecular weight of the kallikrein was calculated to be 29,000 by gel-filtration on a column of Sephadex G-50. The kallikrein was stable between pH 6 and 11 and hydrolysed Pro-Phe-Arg-MCA optimally at pH 11.0. The Pro-Phe-Arg-MCA hydrolysing activity of rat stomach kallikrein was inhibited by DFP and Trasylol, but not by trypsin inhibitors from soyabean, limabean and ovomucoid. These properties of rat stomach kallikrein was clearly distinguishable from those of partially purified rat plasma kallikrein, but similar properties to other glandular kallikreins from other species. From these results, it was concluded that kallikrein is present in rat stomach, which can be classified into glandular kallikrein.
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PMID:Rat stomach kallikrein: its purification and properties. 49 18

Leukocytes contain within their lysosomal granules enzymatic activity that will generate from C5 chemotactic activity for leukocytes (neutrophils) and tumor (Walker carcinosarcoma) cells. Similar activity has been found in phagocytic supernatant fluids from neutrophils and in purified preparations of the leukocyte neutral proteases elastase and cathepsin G. White leukotactic activities can be generated from either the third (C3) or the fifth (C5) components of complement, only C5 serves as a source for generation of the chemotactic activity for tumor cells. As has been previously shown with trypsin, the C5-related chemotactic activities generated by leukocyte proteases are time-dependent: leukotactic activity appears early, then disappears, and is replaced by chemotactic activity for tumor cells. The generation of these chemotactic activities from C5 is blocked by prior treatment of leukocyte preparations with the neutral protease inhibitor Trasylol. The demonstration that enzyme activities from leukocytes have the ability to generate tumor cell chemotactic factors from C5 suggests a possible mechanism by which the development of metastatic lesions may be promoted at sites of tissue injury or inflammation.
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PMID:Digestion of the fifth component of complement by leukocyte enzymes. Sequential generation of chemotactic activities for leukocytes and for tumor cells. 56 81

Using an assay of macrophage migration, where the cells emigrate from an agarose droplet, it was found that the neutral proteases trypsin, chymotrypsin, Pronase and elastase have MIF-like activity. Appropriate enzyme inhibitors counteract this effect. To twelve synovial fluids from patients with inflammatory arthritis, which have MIF-like activity (migration index between 0-3 and 0-7) protease indhibitors (Trasylol, ovomucoid and soybean inhibitor) were added. Ten of the fluids lost some of their MIF-like activity with at least one inhibitor. Phenylmethylsulphonylfluoride counteracted totally the MIF-like activity of the two fluids tested. It is concluded that MIF-like activity of inflammatory synovial fluids is due, at least partially, to proteases.
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PMID:Migration inhibition factor-like activity in inflammatory synovial fluids might be due to proteases. 79 49

Isolation of tropoelastin is complicated by the presence of a neutral protease closely associated with tropoelastin that is capable of sequentially degrading tropoelastin to small peptides. Substrate and inhibitor specificities of this neutral protease associated with purified tropoelastin were examined. The enzyme displayed proteolytic activity against casein, and esterase activity was detected when assayed against N-tosyl-L-arginine methyl ester but not against tert-butyl-oxycarbonyl-L-alanine p-nitrophenyl ester. No appreciable elastinolytic activity was detectable against either insoluble sodium dodecyl sulfate treated elastin or maleylated tropoelastin. The enzyme was not inhibited by the chymotrypsin inhibitor toluenesulfonylphenylalanine chloromethyl ketone. The enzyme was inhibited by phenylmethanesulfonyl fluoride and, to various degrees, by metal chelators. Tosyllysyl chloromethyl ketone, epsilon-aminocaproic acid, and Aprotinin (pancreatic trypsin inhibitor--Kunitz type), all inhibitors of trypsin-like enzymes, were very effective inhibitors, as were soybean trypsin inhibitor and human alpha-1-antitrypsin. The data suggest that the tropoelastin-associated enzyme is a neutral serine protease with trypsin-like specificity.
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PMID:Trypsin-like neutral protease associated with soluble elastin. 90 57

Beside other digestion enzymes the crayfish Cambarus affinis SAY possess an anionic trypsin. This enzyme could be separated from all the other proteins of the crude gastric juice by a single affinity chromatographic step on immobilized natural inhibitor. The dissociation of the thus produced enzyme-inhibitor complex was achieved by specific elution with ben-amidine. The soluble benzamidine-trypsin-complex was dialyzed and separated by gelfiltration on Sephadex G-50. Of the ligands used Trasylol proved to be the most effective one. Trypsin isolated by this ligand was in a discelectrophoretic homogeneous state. On the other hand, trypsin purified by Soybean trypsin inhibitor and Contrykal contains impurities.
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PMID:[Purification of an anionic trypsin from the gastric juice of the crayfish Cambarus affinis say by means of affinity chromatography]. 108 6

The in vivo effect of purified human alpha1-antitrypsin and inter-alpha-trypsin inhibitor on the fertilizing ability of capacitated rabbit spermatozoa was investigated and compared with that of the trypsin-kallikrein inhibitor from bovine organs (Trasylol). Only 250 mug of alpha1-antitrypsin/5 X 10(4) sperm in 0.05 ml inhibited fertilization by more than 50%. Lower concentrations of alpha1-antitrypsin (50 mug/5 X 10(4) sperm in 0.05 mo) and inter-alpha-trypsin inhibitor in amounts of 250 mug/5 X 10(4) sperm and less had no significant effect on the fertilization rate. Comparative experiments with Trasylol in conentrations of 50 mug/5 X 10(4) sperm resulted in more than 50% fertilization inhibition, whereas 100 mug/5 X 10(4) sperm decreased the fertilization rate by approximately 90%. The differences in the antifertility effect of these acrosin inhibitors toward capacitated spermatozoa may be due to differences in molecular weight. The effective concentrations required for fertilization inhibition appear to be relatively high under the experimental conditions used.
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PMID:Effect of serum proteinase inhibitors on the fertilizing capacity of rabbit spermatozoa. 108 94

The purification of rabbit pancreatic trypsin (EC 3.4.21.4) by affinity chromatography on Trasylol-Sepharose is presented along with its physical, chemical and immunological relationship to other trypsins. The molecule is a single polypeptide chain, which immunologically cross-reacts with porcine trypsin, but not with rabbit acrosomal proteinase. Sequence homology with other mammalian trypsins is seen at the amino terminus.
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PMID:Purification and properties of rabbit trypsin. 108 71

Human urinary kallikrein [EC 3.4.21.8] (HUK) was purified about 200-fold with an overall yield of 40 percent from crude powder by DEAE-cellulose chromatography, acetone fractionation, Sephadex G-100 gel filtration and DEAE-Sephadex A-50 chromatography. Its activity was 200 kallikrein units (KU) per A280. HUK from active fractions obtained by DEAE-Sephadex A-50 chromatography was separated into three active components showing isoelectric points of 3.9 (HUK-1), 4.0 (HUK-2), and 4.2 (HUK-3) by isoelectric focusing: each HUK component was homogeneous on disc electrophoresis. The approximate molecular weights of HUK-1, -2 and -3 were estimated to be 2.7 X 10(4), 2.7 X 10(4), and 2.9 X 10(4), respectively, by gel filtration on a Sephadex G-100 column. The optimum pH's of HUK-1, -2, and -3 in esterolytic action were found to be 8.0, 8.3, and 7.5, respectively, and they were fairly heat stable in comparison with other glandular kallikreins. The three components of HUK were weakly inhibited by Trasylol, but were not affected by soybean and ovomucoid trypsin inhibitors. They were strongly resistant to treatment with urea and weakly resistant to treatment with guanidine. The activation energies of HUK-1, -2, and -3 were found to by 1.17 X 10(4), 5.1 X 10(3), and 1.45 X 10(4) cal per mole, respectively. The Km values were estimated toward N-alpha-tosyl-L-arginine methyl ester (TAME), N-alpha-benozyl-L-arginine ethyl ester (BAEE), and N-alpha-benozyl-L-arginine methyl ester (BAME).
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PMID:Studies on urinary kallikreins. I. Purification and characterization of human urinary kallikreins. 108 37

Plasma membranes prepared from rat renal cortex contain both a parathyroid hormone-sensitive adenylate cyclase and a potent proteolytic activity which degrades the hormone into peptide fragments. The degree and pattern of degradation was determined by subjecting incubation mixtures to gel filtration and ion exchange chromatography. Estimation of the degree of degradation by acid precipitation of the intact hormone was inadequate since metabolism of the hormone apparently generated acid-insoluble fragments. When parathyroid hormone was incubated with membrane fraction, the capacity of its stimulatory effect on adenylate cyclase decreased steadily. This decrease of PTH activitiy could be closely related to the degradation of intact hormone by the same membrane preparation. The adenylate cyclase and degradative activity appeared to exist in similar membrane structures since they could not be separated by centrifugation through sucrose density gradients. The degradation of the hormone could not be inhibited by Trasylol and pancreatic or soybean trypsin inhibitors and was only slightly inhibited by ribonuclease and benzamidine. Histone (1 mg per ml), on the other hand, was able to decrease the degradation of the hormone and prevent the loss of its activity. Radioimmunoassay of the incubation mixtures showed that the rapid degradation of both amino- and carboxy-terminal regions of the hormone was prevented by histone. The oxidized, inactive hormone was also degraded to the same extent by the renal cortical membrane. Furthermore, the degradative activity was also found in plasma membrane preparations of renal medulla and liver. This lack of hormone and tissue specificity suggests that similar degradative activity exists in all tissues and that caution should be exercised in estimating hormonal potency based on activation of adenylate cyclase.
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PMID:Interaction of parathyroid hormone with membranes of kidney cortex: degradation of the hormone and activation of adenylate cyclase. 119 1

Two alkaline proteases, one splitting preferentially the substrates of chymotrypsin (ATEE) and the other one those of trypsin (BAEE), were separated and partially purified by chromatographic means from human skin extract made in a buffer containing 1.07 mol/1 KC1. The proteins soluble in dilute buffer were removed by a prior extraction. The enzymes could be separated effectively only in the presence of KC1 at a high conc-ntration since large molecular size aggregates or polymers were formed in solutions of low ionic strength. In the presence of 2 mol/1 KC1 the molecular size of the BAEE-hydrolysing enzyme was 120000 and that of the ATEE-hydrolysing enzyme 30000. The ATEE-hydrolysing enzyme was purified by Sephadex G-100 gel filtration and DEAE-cellulose chromatography about 250 fold. It also hydrolysed esters of tryptophane and phenylalanine as well as casein with optimum pH 7.8--8.2. The enzyme was inhibited effectively by LBTI, SBTI and partially by trasylol, TPCK and TLCK, but not by E-600 and SH-modifers. The hydrolysis of ATEE was doubled in the presence of 1 mol/lKCl, NaCl, KBr or NaBr but that of casein was inhibited to some extent. Human serum and alpha-1-antitrypsin inhibited this enzyme but not C1-inactivator. alpha-2-Macroglobulin did not protect if from inhibition by SBTI. The BAEE-hydrolysing enzyme was purified by Sephadex G-100 gel filtration and hydroxylapatite chromatography about 30 fold. It also split other esters of substituted basic amino acids as well as BAPA and histone proteins with optimum pH 7.5--8.2. It was inhibited by Trasylol and TLCK, but not by LBTI, SBTI, OMTI, TPCK, E-600, SH-modifiers, human serum, C1-inactivator or alpha-1-antitrypsin. Neither of these enzymes is exactly similar to any one of the enzymes so far separated from human tissues or fluids.
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PMID:Human skin proteases: separation and characterization of two alkaline proteases, one splitting trypsin and the other chymotrypsin substrates. 120 Jul 4


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