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)

The covalent structure of the first 111 residues from the N-terminus of peptide alpha1(II)-CB10 from bovine nasal-cartilage collagen is presented. This region comprises residues 552-661 of the alpha1(II) chain. The sequence was determined by automated Edman degradation of peptide alpha1(II)-CB10 and of peptides produced by cleavage with trypsin and hydroxylamine. Comparison of this region of the alpha1(II) chain with the homologous segment of the alpha1(I) chain indicated a homology level of 85%, slightly higher than that of 81% reported for the N-terminal region of the alpha1(II) chain (Butler, Miller & Finch (1976) Biochemistry15, 3000-3006). The occurrence of two residues of glycosylated hydroxylysine was established at positions 564 and 603, the first present exclusively as galactosylhydroxylysine and the latter as a mixture of galactosylhydroxylysine and glucosylgalactosylhydroxylysine. Also, two residues at positions 648 and 657 were tentatively identified as glycosylated hydroxylysines. The amino acid sequences adjacent to the hydroxylysine residues so far identified in the alpha1(II) chain were compared with the homologous regions of the alpha1(I) and alpha2 chains, but no obvious prerequisite for hydroxylation could be seen. From comparison with the homologous sequence of the alpha1(I) chain, it appears that the alpha1(II)-chain sequence presented here contains three more amino acids than that reported for the alpha1(I) chain. This triplet would be interposed between residues 63 and 64 of the reported sequence of peptide alpha1(I)-CB7 from calf skin collagen. Data on the purification of the subpeptides and their amino acid compositions have been deposited as Supplementary Publication SUP 50087 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.
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PMID:The covalent structure of cartilage collagen. Amino acid sequence of residues 552-661 of bovine alpha1(II) chains. 74 39

A procedure involving mechanical agitation referred to as vortexing is compared to a trypsin procedure for obtaining myogenic cells for culture. The vortex procedure appears to be at least as useful as the trypsin procedure and has several advantages including speed, the elimination of chemical disruptive agent, elimination of collagen coating of culture dishes and earlier onset of fusion.
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PMID:A simplified procedure for preparing myogenic cells for culture. 78 9

Allogeneic dermal collagen has been evaluated as an alternative to skin autografts for the permanent replacement of lost or damaged skin in the rat. All non-collagenous structures were removed from full-thickness back skin by treatment with a solution of crystalline trypsin. Such dermal collagen preparations were grafted into skin wounds, examined up to 8 1/2 weeks after operation, and compared with excised wounds and skin isografts and allografts of the same initial size. The dermal collagen grafts, particularly when dressed with a sheet of dermal collagen, become recellularised, revascularised and re-epidermalised. Unlike the skin allografts, there was no evidence of cellular rejection. Whereas contracture of the excised wounds was delayed, but not suppressed, by applying a conventional dressing, collagen grafts maintained from 60 to 100 per cent of their original size. In contrast, equivalent skin isografts shrank to 50-60 per cent and showed persistent epidermal hyperplasia.
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PMID:Incorporation of stored cell-free dermal collagen allografts into skin wounds: a short term study. 83 88

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

A topographical study of the articular surface of 21 femoral heads removed for surgery of osteoarthrosis was made using the scanning electron microscope. Sections of degenerate cartilage were pretreated with H2O2 and trypsin to reveal the collagenous framework. Torn and frayed collagen bundles were evident on all the specimens studied, the length of these bundles varying from 20 to 150 micron. The frequency of the bundles over the degenerate fibrous areas varied considerably, and bundle sizes ranged from 20 to 70 micron. The topography of a single femoral head removed from a rheumatoid arthritic was very much smoother, with torn fibre ends ruptured at the same level. Although the exposed bone was considerably "smoother" than the residual fibrocartilage, ruptured osteons and trabeculae revealed large voids in the surface which would presumably alter the lubrication and fluid flow characteristics of the functioning joint. The effects of these changes on joint tension and lubrication are discussed.
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PMID:Osteoarthrotic articular cartilage lesions of the femoral head observed in the scanning electron microscope. 87 41

After an in vitro incubation of platelets with fibrillar collagen, their elastase activity is markedly and rapidly increased while proelastase decrease: proelastase is activated in situ into elastase which is released in its active form from the platelet. The activation of proelastase is likely due to the action of a trypsin-like enzyme present in the platelet. This protease has the same type of localization as proelastase and elastase: their highest activity is associated with light granules but part of these enzymes (or precursor) is also associated with the membranes. The mechanism of the arterial elastolysis induced by the platelets probably involves their adhesion to intimal thrombogenic surfaces (collagen) followed by a reaction during which proelastase would become available to the trypsin-like enzyme and would be activated into elastase directly released in the vessel wall.
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PMID:Human blood platelet elastase and proelastase. Activation of proelastase and release of elastase after ahesion of platelets to collagen. 88 80

Hypercholesterolemia was induced in rats by feeding them a high cholesterol olive oil diet. The livers were homogenized in modified Krebs-Ringer medium and centrifuged at 35,000 x g. The supernatants from livers of both hypercholesterolemic and normal rats were found to stimulate collagen synthesis in freshly isolated embryonic chick-tendon fibroblasts. However, this was significantly greater in the supernatants from fatty livers. The stimulating principle proceed to be dialyzable, non-lipid and heat-stable. There were at least two factors involved, the more effective of which was trypsin-sensitive, with a molecular weight below 2,000. The results suggest that a mediator is formed in the livers of hypercholesterolemic rats which might be responsible for the enhanced collagen synthesis of fibrotic processes vivo, e.g., in atherosclerosis and liver cirrhosis.
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PMID:Factors stimulating collagen synthesis from the livers of hypercholesterolemic rats. 94 25

Scanning electron microscopy was used to study the architectonics of the connective tissue fiber framework in the walls of large arteries. Preliminary treatment of the vascular samples with proteolytic enzymes (protorysin, trypsin) offered a possibility of determining peculiarities attending distribution and interrelations of collagen and elastic fibers in different strata of the vascular wall.
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PMID:[Application of scanning electron microscopy to studying the architectonics of the fibrous framework of the walls of large vessels]. 94 88

Human polymorphonuclear leucocytes were obtained from the synovial fluids of patients with inflamed knee joints suffering either from Reiter's syndrome or from rheumatoid arthritis. The polymorphonuclear leucocytes were collected by gentle centrifugation followed by disruption and their subcellular fractionation by centrifugation in 0.34 M sucrose to provide a granule fraction and a post-granule supernatant fraction. 0.5 M KCl extraction of the granule fraction yielded neutral protease activity, similar to trypsin, when assayed against fluorescein-labelled polymeric collagen fibrils. The post-granule supernatant fraction contained an inhibitor towards the neutral protease and trypsin. The inhibition of the neutral protease was found to be time-dependent, this inhibition being released after 1.5-2 h. In contrast, the inhibition of trypsin was irreversible and this property was used to devise an assay procedure for the inhibitor.
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PMID:Human-polymorphonuclear-leucocyte neutral protease and its inhibitor. Studies with fluorescein-labelled polymeric collagen fibrils as a substrate. 96 37

Binding of a denaturated polypeptide chain derived from chick skin collagen, the alpha 1(I) chain, by isolated membranes of human platelets has been demonstrated. The process is reversible, and time- and protein concentration-dependent. The binding is specific, with an association constant of 1.88 X 10(-6) M. Prior treatment of the isolated membranes with trypsin, chymotrypsin, and pronase, resulted in significant inhibition of the 14C-labeled alpha 1 chain binding, but neuraminidase or collagenase treatment had no effect. Dissociation of the bound radioactivity and subsequent chromatographic analyses on carboxymethylcellulose and agarose A-1.5m revealed that the alpha 1 chain was unaltered. Scatchard plot analysis suggested that there are approximately 20,000 binding sites per platelet. The binding of the alpha 1 chain was inhibited by a glycopeptide derived from alpha 1, alpha 1-CB5 and by purified glucosylgalactosyl hydroxylysine, but was not affected by other cyanogen bromide peptides of alpha 1, namely alpha 1-CB3, -CB4, -CB7, and -CB8. Kinetic studies demonstrated that inhibition by the hydroxylysine glycoside is competitive. Dose-response curves of platelet aggregation induced by alpha 1 and the binding of alpha 1 by platelet membranes correlate closely. These results indicate that there are specific binding sites for collagen alpha 1 chain on platelet membranes, and that the carbohydrate moiety of the alpha 1 chain plays a role in the binding. The findings also support the hypothesis that the chick skin alpha 1 chain mediates platelet aggregation and the release reaction by acting on platelet membranes.
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PMID:Binding of chick skin collagen alpha 1 chain by isolated membranes from human platelets. 97 74


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