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)

Potassium thiocyanate inhibited the activities of trypsin and chymotrypsin. The inhibition was mixed type on both enzymes with casein as substrate and on trypsin with tosyl-L-arginine methyl ester as substrate, but was uncompetitive on chymotrypsin with benzoyl-L-tyrosine p-nitroanilide as substrate.
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PMID:Modes of inhibition of activities of trypsin and chymotrypsin by potassium thiocyanate. 51 Feb 80

A number of fractions with differing intensity of the inhibitory action on the gastric secretion were obtained by gel filtration in a column with biogels P-30 and P-2 of cappa-casein glycomacropeptide. A low-molecular fraction displays the greatest capacity for inhibiting gastric secretion. Desialism, heating and partial hydrolysis of glycomacropeptide with pepsin, trypsin and chemotrypsin used separately have no effect on its inhibitory activity. The resulting data suggest that the inhibitory action of glycomacropeptide is caused by a certain part rather than by entire molecule.
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PMID:[Heterogeneity of the kappa-casein glycomacropeptide and physiological activity of its fractions]. 51 96

A procedure for preparing derivatives of dialdehyde dextran-glass-carriers and their use for immobilization of trypsin is described. The dextran to the support as well as the trypsin to dextran were covalently immobilized via dialdehyde groups. The relative activity of immobilized trypsin in these enzyme-carrier-complexes amounted 17.3% and 20,4 (determined with alpha-N-Benzoyl-DL-arginine-p-nitroanilid) and 8,2% and 11.6% (determined with casein).
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PMID:[Synthesis and properties of insolubilized enzyme. XI. Trypsin-carrier-complexes on the basis of macroporous glasses by interposing the hydrophilic polymer dextran]. 51 95

Ca(2+)-activated neutral proteinase was purified from rabbit skeletal muscle by a method involving DEAE-Sephacel chromatography, affinity chromatography on organomercurial-Sepharose and gel filtration on Sephacryl S-200 and Sephadex G-150. The SDS (sodium dodecyl sulphate)/polyacrylamide-gel-electrophoresis data show that the purified enzyme contains only one polypeptide chain of mol.wt. 73000. The purification procedure used allowed us to eliminate a contaminant containing two components of mol.wt. about 30000 each. Whole casein or alpha(1)-casein were hydrolysed with a maximum rate at 30 degrees C, pH7.5, and with 5mm-CaCl(2), but myofibrils were found to be a very susceptible substrate for this proteinase. This activity is associated with the destruction of the Z-discs, which is caused by the solubilization of the Z-line proteins. The activity of the proteinase in vitro is not limited to the removal of Z-line. SDS/polyacrylamide-gel electrophoresis on larger plates showed the ability of the proteinase to degrade myofibrils more extensively than previously supposed. This proteolysis resulted in the production of a 30000-dalton component as well as in various other higher- and lower-molecular-weight peptide fragments. Troponin T, troponin I, alpha-tropomyosin, some high-molecular-weight proteins (M protein, heavy chain of myosin) and three unidentified proteins are degraded. Thus the number of proteinase-sensitive regions in the myofibrils is greater than as previously reported by Dayton, Goll, Zeece, Robson & Reville [(1976) Biochemistry15, 2150-2158]. The Ca(2+)-activated neutral proteinase is not a chymotrypsin- or trypsin-like enzyme, but it reacted with all the classic thiol-proteinase inhibitors for cathepsin B, papain, bromelain and ficin. Thus the proteinase was proved to have an essential thiol group. Antipain and leupeptin are also inhibitors of the Ca(2+)-activated neutral proteinase.
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PMID:Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle. 53 1

Casein epsilon-aminolysyl residues were converted to the methyl (and dimethyl), isopropyl or cyclopentyl derivatives in high yield with formaldehyde, acetone or cyclopentanone, respectively, in the presence of sodium borohydride. When incorporated into diets at 10% as the sole protein source, the chemically modified caseins failed to support growth of young rats. Methyl casein did, however, support limited growth after about 5 days. Plasma threonine levels increased and lysine levels decreased markedly in rats fed the alkyl caseins. The respective alkyllsine derivatives were present in plasma and urine. In another experiment, nearly normal or normal growth was obtained by feeding lysine-supplemented methyl or isopropyl casein, respectively. A preparation of partially methylated casein, containing approximately equal amounts of monomethyl- and dimethyllysines, supported normal rat growth. These results demonstrate that lysine deficiency was produced by feeding highly alkylated caseins. Digestibility of the chemically modified caseins in vivo was not affected, although in vitro studies with trypsin and alpha-chymotrypsin showed lowered digestibility. Since no apparent toxicity was observed limited methylation of food proteins may be useful for protection of lysyl residues against deteriorative reactions during processing and storage.
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PMID:Effect of reductive alkylation of the epsilon-amino group of lysyl redsidues of casein on its nutritive value in rats. 56 44

Human milk casein samples were digested with trypsin and chymotrypsin, and a glycopolypeptide fraction was isolated from the soluble portion of the digests by a series of gel filtration steps. The glycopeptide fraction stimulated the growth of Lactobacillus bifidus subspecies pennsylvanicius to the same extent as a whey glycopolypeptide fraction previously isolated (Pediat. Res. 10: 1, 1976). It contained between 60 and 70% carbohydrate consisting of galactose, galactosamine, glucosamine, fucose, and sialic acid. This, along with its apparent molecular weight of near 30,000 was also similar to the respective parameters of the whey glycopolypeptide. It is proposed that human milk casein may serve a dual function: that serving the nutritional needs of the breast-fed infant, and that stimulating the growth of L. bifidus subspecies pennsylvanicus. Additionally, the whey glycopolypeptide may arise from casein through proteolysis by an endogenous milk protease.
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PMID:Isolation of a glycopolypeptide fraction with Lactobacillus bifidus subspecies pennsylvanicus growth-promoting activity from whole human milk casein. 57 32

Effect of penicillin, kanamycin and streptomycin on the proteolytic activity of trypsin using hemoglobin and casein as substrates as well as effect of these antibiotics and oxacilin, methycillin and tetracycline on the lipase activity were studied in vitro. Penicillin, kanamycin and streptomycin (5 mg, 20 mg and 80 mg of the antibiotic per 1 mg of trypsin, respectively) did not inhibit the proteolytic activity of the enzyme. Kanamycin slightly activated the trypsin activity in reaction with hemoglobin and streptomycin -- in reaction with casein. Penicillin, oxacillin and methycillin inhibited the lipase activity, when 80-100 mg of the antibiotics were used per 1 mg of the enzyme.
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PMID:[Trypsin and lipase activity in the presence of antibiotics]. 59 96

This study was directed toward demonstrating an interaction between human polymorphonuclear leukocytes (PMNs) and the chemotactic factor,casein. Experiments conducted using fluorescein-labeled casein indicated that PMNs have a membrane receptor for this chemotactic factor. This receptor was specific for casein and was not found on lymphocytes. A direct parallel was shown between the binding of FITC--casein and the PMN chemotactic response to this protein. Binding to the receptor was optimal at 25 degrees C, unaffected by sodium azide, and partially reduced by iodoacetate. Enzymatic treatment of PMNs with pronase and trypsin resulted in a loss of both FITC--casein-mediated PMN fluorescence and chemotaxis. Our data indicate that human PMNs have a membrane receptor for casein and that interaction with this receptor results in a chemotactic response.
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PMID:Casein-mediated neutrophil chemotaxis: a parallel between surface binding and chemotaxis. 61 3

The major component of the casein fraction of human milk was cleaved by cyanogen bromide, and the composition of the resulting peptides was determined. Casein was also subjected to limited digestion by trypsin, and the amino acid composition of the isolated peptides was established. With this information the peptides were ordered as they occur in the purified protein.
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PMID:Isolation, composition and ordering of cyanogen bromide peptides in human casein. 62 58

Casein was modified by use of a series of active N-hydroxy-succinimide esters of amino acids in order to study the effects of new covalently linked hydrophobic or hydrophilic groups on its physical and nutritional properties. Tryptophan was used to determine the best conditions for the chemical reaction and to study the stability of the newly formed amide linkage (isopeptide bond). Casein was also modified with glycine, alanine, methionine, N-acetyl-methionine and aspartic acid. In vitro hydrolysis studies using bovine chymotrypsin, pancreatine and rat bile-pancreatic juice indicated that digestibility of the modified casein derivatives was lower than that of the untreated protein. Since solubility was not significantly changed (except for tryptophyl-casein), the decreased in vitro digestibility is probably due to other factors such as steric hindrance as well as decrease in lysine residues available to trypsin in pancreatin and rat pancreatic juice. Plasma amino acid patterns for rats fed a 10% protein diet of highly modified glycyl-casein or methionyl-casein suggest that the epsilon-aminolysyl derivatives are readily hydrolyzed in vivo. This was confirmed by the growth response of rats fed the following isonitrogenous diets (protein source listed only): casein, casein + free methionine, methionyl-casein, casein + free N-acetyl-methionine, N-acety-methionyl-casein. Covalently attached methionine appeared to be as readily available as the free amino acid; bound N-acetyl-methionine was also available but to a slightly lower extent. Although this study is preliminary, the covalent attachment of amino acids to proteins appears to be a promising method for improving the biological value of food proteins.
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PMID:A method for improving the nutritional value of food proteins: covalent attachment of amino acids. 72 27


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