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:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human monocytes, when appropriately stimulated in vitro, release into the culture medium a factor (BAF) that stimulates the IgM response of T-depleted murine splenocytes to heterologous erythrocytes. The behavior of this factor on gel filtration, isoelectric focusing, ion exchange chromatography, and isopycnic centrifugation was studied. BAF appears to be a molecule of 15,000 daltons, pI 6.5, 1.33 g/ml with low solubility at low ionic strength. It is stable to acid, mild heating, and long-term storage. Activity is lost in alkali or by boiling. Papain may reduce BAF activity slightly, whereas trypsin and chymotrypsin have no significant effect. These properties are similar to those of other monokines reported to have a similar m.w.
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PMID:Purification and properties of human B cell-activating factor. 3 65

Keratan sulfate-rich peptides were isolated after digestion of proteoglycans from bovine nasal cartilage and bovine nucleus pulposus with chondroitinase ABC, trypsin and chymotrypsin. The keratan sulfate enriched peptides from nucleus pulposus were larger than those from nasal cartilage. Keratan sulfate chains were isolated after treatment of the keratan sulfate-rich peptides under alkaline, reductive conditions. Proteoglycans from nucleus pulposus contain longer keratan sulfate chains, as is shown primarily by gel chromatography of the keratan sulfate-rich peptides and the keratan sulfate chains, but also from end-group analyses of the keratan sulfate chains.
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PMID:Skeletal keratan sulfate from different tissues. Characterization and alkaline degradation. 4 89

The trypsin and chymotrypsin inhibitor from chick peas (CI) is stable in HCl 0.001 M -- 0.01 M and in KOH 0.01 M -- 0.05 M even after 24 h. Increased KOH concentrations decrease considerably the inhibitory activity already after 1 h. Maleyation and succinylation of the inhibitor resulted in almost full loss of its trypsin-inhibitory activity but had no effect on the chymotrypsin-inhibitory activity. A series of modifications directed towards tyrosyl residues showed that iodination influenced only the chymotrypsin-inhibitory activity; however, nitration and arsanilation affected not only the chymotrypsin-inhibitory activity but also the trypsin-inhibitory activity. Treatment of the inhibitor with CNBr and chloramine T resulted only in a decrease in the chymotrypsin-inhibitory activity indicating that the only methionine is involved in the chymotrypsin-inhibitory activity. When CI-fragment A, previously treated with trypsin at pH 3.75, was further treated with carboxypeptidase B, a release of three lysyl residues per mole protein was found. CI was separated by equilibrium chromatography on SP-Sephadex column into two isoinhibitors, CII and CIII, respectively. Both inhibited trypsin and chymotrypsin with the same specific activity as CI. They differed from each other only in a glutamyl, aspartyl, glycyl and alanyl residue.
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PMID:Trypsin and chymotrypsin inhibitor from chick peas. Selective chemical modifications of the inhibitor and isolation of two isoinhibitors. 4 22

Large quantities of the low-molecular-weight natriuretic material (F4), which appears after the salts when fractionated on G-25 Sephadex column, were obtained from the urine of normal man on a normal diet. The natriuretic substance in F4 was (1) untrafiltrable through a membrane with a claimed molecular-weight cut-off of 500 daltons (Amicon UMO5); (2) soluble in more polar organic solvents; (3) totally soluble in 95% acetone when specific activity was doubled; (4) relatively resistant to heating at 100 degrees C for 1 hour at a pH of 10, and to heating at 110 degrees C in 6 N hydrochloric acid for up to 90 hours under anaerobic conditions, and treatment with nitrous acid; it was less resistant to these procedures when extracted into 95% acetone; (5) not destroyed by trypsin, chymotrypsin, pronase, pepsin, leucine aminopeptidase, and subtilysin, nor was it destroyed by pepsin, leucine aminopeptidase, subtilysin, carboxypeptidase A and B, and aminopeptidase M, or by monoamine oxidase, aryl sulphatase, and beta-glucuronidase when extracted into 95% acetone. The natriuretic substance in the 95% acetone-soluble F4 was totally destroyed by incubation with prolidase. The least amount of 95% acetone-soluble F4 required to produce a significant natriuresis in the bioassay rat was that derived from a 7-min sample of urine. The maximal response was obtained from a 30-min sample of urine. Continuous i.v. infusion of the 95% acetone-soluble F4 for 40 min produced a sustained natriuresis, whereas a greater amount injected as a bolus produced an effect which was not sustained beyond 20 min.
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PMID:Further observations on a low-molecular-weight natriuretic substance in the urine of normal man. 4 87

Highly sensitive gelatin substrate films prepared according to a recent variant of the procedure are studied for their susceptibility to the action of various endopeptidases and exopeptidases. Trypsin, papain, elastase, and chymotrypsin are found to hydrolyze the gelatin films most easily, while higher enzyme concentrations are required in case of pepsin, plasmin and collagenase. The exopeptidases, i.e. leucine aminopeptidase, amino acid arylamidase and carboxypeptidases A and B do not cause lysis of gelatin substrate films. The example of a rabbit blastocyst protease involved in implantation is given to demonstrate the application of gelatin substrate film tests for studies of enzymes which have no or little activity against known synthetic substrates (like BANA or GPNA) but hydrolyze gelatin films. Studies of interactions of this blastocyst protease with various inhibitors of known specificity, however, show that the active center of this enzyme nevertheless has striking similarities to trypsin (and also to chymotrypsin). The enzyme is possibly related to elastase. It is emphasized that, besides this, there are a number of different protease type enzymes in rabbit blastocyst and uterine tissues, some of which can be demonstrated only with chromogenic substrates and some only by gelatin methods. Aspects of applicability of the two types of protease tests are briefly discussed.
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PMID:[The specificity and sensitivity of the gelatin base protease substrate film test ]. 4 23

A 60,000-dalton polypeptide (p60) has been identified in the feline leukemia virus (FeLV) pseudotype of Moloney sarcoma virus [MSV(FeLV)]. This polypeptide is present in the purified virus complex in concentrations greater than either the murine p30 or the feline p27. Purified p60 crossreacts immunologically with murine p30 group antiserum and contains several interspecies determinants, whereas the group specific determinant of FeLV p27 is not detected. Comparison of peptide fingerprints of p60 and murine p30 show many peptides in common. Limited digestion of p60 with either trypsin or chymotrypsin produced p30-35 and p20 peptides which retain the MuLV p30 group and interspecies antigenic activities. The p30 produced by both enzymes comigrates in polyacrylamide gels with the murine p30 of MSV(FeLV), thus suggesting that p60 may be an uncleaved precursor to p30.
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PMID:A p60 polypeptide in the feline leukemia virus pseudotype of Moloney sarcoma virus with murine leukemia virus p30 antigenic determinants. 4 60

Three phenotypical variants of normal human serum alpha2-macroglobulin revealed by immunoelectrophoresis and specific antibodies obtained in rabbits are presented. The variants are characterized by differences in electrophoretic mobility: one being fast, one slow, and one of an intermediate rate. To find out possible differences with respect to the effect of the trypsin and chymotrypsin on the three variants, they were treated with the enzymes before immunoelectrophoresis. Migration was accelerated in all cases, after complexing with the enzymes, but the differences in the relative positions of the variants were maintained. The trypsin- and chymotrypsin-binding capacities of these three forms seem to differ, as suggested by the results presented in this report.
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PMID:Variants of normal human alpha2-macroglobulin. Immunoelectrophoresis and enzyme-binding effect. 5 Feb 67

Pancreatitis was induced by injection of autologous bile into the main pancreatic duct of dogs. An initial fall in blood pressure was accompanied by appearance of large quantities of active trypsin, chymotrypsin, and elastase in pancreatic exudate with full saturation of protease inhibitors. The enzymes soon appeared in ascitic fluid and lymph, but only in the form of complexes with alpha1-antitrypsin, and alpha2-macroglobulin. No such complexes were detected in venous blood indicating short half-life in the circulation. These studies confirm the release of pancreatic enzymes during bile-induced pancreatitis, and quantify an important protective role for plasma protease inhibitors in this situation.
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PMID:Release of proteolytic enzymes in bile-induced pancreatitis in dogs. 5 Sep 58

Human leukocytes, when exposed to aggregated human gamma-globulin (AHGG) or immune complexes (isolated from RA synovial fluid) fixed to a cartilagenous surface, release neutral proteases that degrade the extracellular matrix of cartilage. The chondromucoprotein destruction by these proteases is suppressed by a variety of synovial fluids but is not susceptible to inhibition by trypsin, chymotrypsin, elastase inhibitors, or a combination of these agents. The inhibitory effect of synovial fluid can be reversed in the presence of increasing enzyme concentrations. Intact viable human polymorphonuclear leukocytes in the presence of AHGG also release a collagenase precursor that can be activated by limited proteolysis with trypsin or RA synovial fluids. Enzyme release (neutral proteases) by phagocytosing cells is inhibited by the antiinflammatory agents phenylbutazone and colchicine; these agents do not affect release of the collagenase precursor. However, the latent collagenase release is susceptible to inhibition when leukocytes are preincubated (prior to exposure to AHGG) with inhibitors of protein synthesis. Under these conditions, neutral protease release is unaffected.
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PMID:Connective tissue-degrading enzymes of human leukocytes. 5 2

A fragment of IgE with molecular weight of about 40,000 was identified by radioimmunoassay in human small intestinal fluid after fractionation by gel filtration chromatography. Digestion of E myeloma protein PS by pooled intestinal fluid, trypsin or chymotrypsin yielded a degradation product of similar molecular weight that probably consisted principally of epsilon 1 determinant-containing fragments. These findings suggest that IgE is secreted into the intestinal lumen and degraded there by pancreatic proteolytic enzymes, producing an enzyme-resistant portion of the amino-terminal part of the Fc region.
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PMID:Studies on IgE in human intestinal fluids. 5 26


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