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)

Salivary and pancreatic lipases of the pre-ruminant calf have been studied using ion-exchange chromatography and gel filtration. In addition, pancreatic lipase has been fractionated using concanavalin A-affinity chromatography. The effects of 5,5'-dithiobis(2-nitrobenzoic acid), organic solvents and trypsin on pancreatic lipase have also been investigated. The effects of taurodeoxycholate on the lipolytic activity of the 2 lipases has been compared. Salivary lipase behaved as a single enzyme on ion-exchange chromatography, and gel filtration gave a mol. wt value of 52,000 for the enzyme. Although pancreatic lipase appeared to be a single enzyme on gel filtration, with a mol. wt of almost 80,000, the lipase was shown by ion-exchange and affinity chromatography to consist of at least 2 enzymes of mol. wts 72,000 and 60,000, and did not require colipase for maximum activity in the presence of high concentrations of bile salts. Colipase-dependent lipase, mol. wt about 45,000, and probably amounting to not more than 10% of the total activity, was also present. This was the predominant form only after large losses in total lipolytic activity had occurred, as after treatment with a mixture of ether, ethanol and deoxycholate, or prolonged action of trypsin. When the concentration of taurodeoxycholate was increased from zero to 1 mM in a tributyrin substrate, the lipolytic activities of calf salivary and pancreatic lipases, and pig pancreatic lipase, increased. At a concentration of 4 mM-taurodeoxycholate, calf salivary lipase activity was higher, that of calf pancreatic lipase lower and pig pancreatic lipase activity markedly lower.
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PMID:Studies on salivary and pancreatic lipases of the pre-ruminant calf. 714 23

The adhesive glycoprotein fibronectin has been isolated from fresh hamster plasma by affinity chromatography on gelatin coupled to Sepharose beads by the method of Engvall & Ruoslahti [Int. J. Cancer (1979) 20, 1-5]. Polyacrylamide-gel electrophoresis of material heated in sodium dodecyl sulphate and 2-mercaptoethanol shows two prominent polypeptide subunits of approx. mol.wts. 215 000 and 200 000, with variable amounts of lower-molecular-weight fragments. The unexpected polypeptide heterogeneity of different preparations of hamster fibronectins and bovine serum fibronectin is shown to be partly an artefact and is generated during isolation and storage of purified fibronectin. Treatment of each hamster fibronectin subunit or a smaller fragment of approx. mol.wt. 140 000 with thermolysin or trypsin after radioiodination produces similar patterns of tyrpsine-containing peptides, indicating similar primary amino-acid sequences. Antibodies raised against the major subunits of hamster plasma fibronectin were coupled to Sepharose beads and used in conjunction with gelatin affinity chromatography to isolate fibronectins extracted with urea from baby-hamster kidney (BHK) cells and present in the long-term culture medium of these cells. The cell and medium fibronectins are similar to hamster plasma fibronectin in amino-acid and carbohydrate composition and also produce very similar peptide 'maps'. We conclude that the various forms of hamster fibronectins are structurally analogous in agreement with indistinguishable biological properties in mediating the substance adhesion of BKH cells [Pena & Hughes (1978) Cell Biol. Int. Rep. 3, 339-344].
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PMID:Polypeptide heterogeneity of hamster and calf fibronectins. 745 16

Two kinds of proteinases, type-I and type-II, were purified or partially purified from salted muscle of anchovy, Engraulis japonica. Mol. wts. of type-I and type-II proteinases were estimated to 25,000 and 37,000, respectively, on electrophoretic analysis. Both proteinases strongly hydrolyzed synthetic tri or tetrapeptide substrates specific to trypsin, alpha-thrombin, and an activated protein C, while they hardly hydrolyzed Arg-MCA and benzoyl Arg-MCA derivatives. The proteinases were inhibited by common trypsin inhibitors. Optimal pH for the proteinase activities were pH 6.8 (type-I) and pH 7.0 to 7.5 (type-II), and the proteinases showed the highest activities at 45 degrees C (type-I) and 50 degrees C (type-II). The N-terminal amino acid sequence of type-I proteinase, 1I-2V-3G-4G ... (29 residues were identified), was significantly similar to sequences of trypsins and tryptases. Based on these findings, both proteinases were presumed to be kinds of tryptases in E. japonica muscle.
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PMID:Two kinds of neutral serine proteinases in salted muscle of anchovy, Engraulis japonica. 761 98

In a search for nerve growth factor (NGF) in tissue extracts of a murine transplantable teratocarcinoma that harbours immature neural tissue in abundance, a trypsin-sensitive and heat labile neurotrophic activity was identified. The final protein fraction obtained by cation exchange chromatography contained five proteins with mol. wts ranging from 52 to 72 kD. It supported the growth and differentiation of immature neurones in neonatal rat cerebellar cultures but had no effect on embryonic chick dorsal root ganglia which are the classical targets for NGF.
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PMID:A teratocarcinoma-derived neurotrophic activity. 766 6

Three distinct alpha 2PI (alpha 2-antiplasmin) degrading and alpha 2M (alpha 2-macroglobulin) inhibiting enzymes, named proteinase a, b and c, have been purified from the venom of Crotalus basiliscus (the Mexican west coast rattlesnake) by fast protein liquid chromatography (anion-exchange chromatography and gel filtration chromatography). SDS-PAGE revealed that proteinase a and b had similar mol. wts (approximately 23,500), whereas proteinase c displayed a mol.wt of approximately 24,200. Their isoelectric points were found to be acidic, ranging from pH 4.8 to 5.7. The proteinase activity of all three enzymes was inhibited in the presence of EDTA. Dependent on enzyme concentration, a progressive and catalytic inactivation of alpha 2PI was induced, leading to an almost complete loss of the plasmin inhibitory activity at a molar ratio of enzyme: alpha 2PI = 0.1 within 60 min. The ability of alpha 2M to protect the esterolytic activity of trypsin from inhibition by soybean trypsin inhibitor was only reduced at a molar ratio of enzyme: alpha 2M = 0.5, whereas no inactivation could be observed when the three venom proteinases were incubated with an excess of alpha 2M, suggesting that the inactivation occurred by complex formation but not by degradation of the intact alpha 2M molecule. In SDS-PAGE, inactivation of human alpha 2PI (mol. wt 68,000) correlated with the appearance of two cleavage products with an approximate mol. wt of 56,000 and 11,000, respectively. The three proteinases had no thrombin-like activity. Plasminogen and factor X were not activated and no platelet aggregation was induced. They degraded the A alpha- and B beta-chain of fibrinogen and showed plasma extravasation-inducing activity following intradermal injection into the abdominal skin. None of the enzymes showed any activity against a series of chromogenic p-nitroanilide substrates.
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PMID:Purification and characterization of three alpha 2-antiplasmin and alpha 2-macroglobulin inactivating enzymes from the venom of the Mexican west coast rattlesnake (Crotalus basiliscus). 859 84


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