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 effect of 1.8 mg/liter (LC50) of mercuric chloride exposure on the activities of alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, amylase, pepsin, trypsin, tripeptidase glycyl-glycine dipeptidase and carnosinase has been examined in Channa punctatus. The three phosphatases have been inhibited in the liver but showed an increase in activity in the intestine and pyloric caeca. Amylase, pepsin and trypsin have also shown a slight increase in activity. There has been no significant alteration in the activites of the peptidases. The results show that mercury inhibits the activites of phosphatases in the liver but has no significant effect on the digestive enzymes within the experimental period of 96 hours.
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PMID:Effect of mercuric chloride on the digestive system of a teleost fish, Channa punctatus. 21 48

Alterations in the activities of alkaline phosphatase, acid phosphatase, glucose-6-phosphatase amylase, trypsin, pepsin, aminotripeptidase, glycylglycine dipeptidase and carnosinase due to exposure of Channa punctatus to a sublethal concentration (0.30 mg/L) of mercuric chloride by bath for 20 days have been studied in the different parts of the digestive system. Afall in the activities of the three phosphatases was recorded except for alkaline phosphatase which showed a slight elevation in activity in intestine and pyloric caeca. An increase in the activity of amylase and the two proteases was observed in all the portions of the digestive system. The three peptidases revealed a decrease in activity.
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PMID:The in vivo effect of mercuric chloride on some digestive enzymes of a fresh water teleost fish, Channa punctatus. 22 1

In vitro studies revealed that the hatching of oncospheres of Moniezia expansa requires the mechanical breakage of the eggshell and subshell membrane and enzymic digestion of the pyriform apparatus. Removal of the outer two egg membranes elicits the activation of most oncospheres. Between pH 5.0-7.8, there is no significant difference in numbers of oncospheres activated by eggshell removal and the addition of sodium bicarbonate has no effect. Solutions of more extreme pH values (2.0 and 10.0) are harmful and render oncospheres immobile. The subshell membrane forms a barrier to the passage of water in an osmotic gradient and to several molecular and ionic substances. Between the eggshell and subshell membrane is a layer of droplets which have a strong affinity for Sudan stains and which are partially removed by lipase. The eggshell is resistant to a variety of proteolytic enzymes, amylases and lipase. The pyriform apparatus is digested by chymotrypsin and pepsin, though not by trypsin. Both eggshell and pyriform apparatus are dissolved by solutions of sodium sulphide and sodium hypochlorite, indicating that their structures are stabilized by disulphide bonds and other covalent linkages.
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PMID:In vitro hatching of the tapeworm Moniezia expansa (Cestoda: Anoplocephalidae) and some properties of the egg membranes. 23 60

The properties of big renin, a relatively inactive form of renin isolated from human plasma, were examined following partial purification by gel filtration. Exposure of big renin to pH 3.0-3.6, or brief incubation with trypsin or pepsin, resulted in a ten-fold increase in enzymatic activity. Activation was not effected by 4M NaCl, 6M urea, or incubation with neuraminidase. Both before and after inactivation, big renin eluted from Sephadex gel more rapidly than normal plasma renin. During polyacrylamide gel disc electrophoresis, inactive big renin migrated more slowly than either normal renin or big renin previously activated. Using sheep substrate, the enzyme kinetics of normal renin and previously activated big renin were identical, while inactive big renin possessed a higher Michaelis constant. These data indicate that big renin is closely related biochemically to normal plasma renin. As the activation of big renin results in the formation of the substance even more similar to normal renin, the possibility exists that big renin may prove to be a precursor form of normal renin.
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PMID:Biochemical properties of big renin extracted from human plasma. 23 15

1. A cyclic hexapeptide, cyclo(-Gly2-Phe2-Gly-Lys-), and the corresponding open-chain hexapeptides, Gly2-Phe2-Gly-Lys and Phe-Gly-Lys-Gly2-Phe, have been synthesized and their susceptibilities to the hydrolytic action of pepsin and trypsin were determined. 2. The cyclic peptide was hydrolyzed slowly by trypsin to a hexapeptide Gly2-Phe2-Gly-Lys, the value of the Michaelis constant for this reaction being Km equals 0.00022 M. 3. The cyclic peptide was not cleaved by pepsin at all, but Gly2-Phe2-Gly-Lys was hydrolyzed rapidly at a Phe-Phe bond; Km equals 0.0091 M. 4. The cyclic peptide inhibits the hydrolysis of Gly2-Phe2-Gly-Lys by pepsin in a linear non-competitive manner, the value of the inhibition constant being Ki equals 0.004 M.
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PMID:Synthesis and hydrolysis by pepsin and trypsin of a cyclic hexapeptide containing lysine and phenylalanine. 24 Jun 80

Eight different types of peptide mixtures from [14C]carboxymethylated yeast alcohol dehydrogenase were obtained using trypsin with or without prior maleylation of the substrate, chymotrypsin, pepsin, microbial proteases or CNBr. Each mixture was fractionated by exclusion chromatography and peptides were further purified on paper. From results of analyses of all fragments it seems possible to to deduce a primary structure of 347 unique residues in three segments. Together, the segments can account for the whole protein monomer with the exception of a small connecting region. Many unfavourable structures complicated the determination and made single sequence conclusions tentative, but known data are consistent and for most segments of the monomer results are abundant. Several microheterogeneities in the protein are indicated and one apparent amino acid exchange is characterized, suggesting that different types of subunits occur. This may probably be correlated with genetic polymorphism in yeast. Multiple desamidations are also characterized and a few of these affect particularly labile structures. Many residues are unevenly distributed and unexpected patterns are shown. Elements of repetitive sequences occur, reducing the uniqueness of structures. Hydrophobic segments are found, and the uncharacterized region is, at least in some subunits, in a core-like tryptic segment. These and other aspects of the structure may explain some properties of the monomer, and form the background for evolutionary, structural and functional correlations with related enzymes.
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PMID:The primary structure of yeast alcohol dehydrogenase. 32

1. The reactivities of phenylglyoxal (PGO), glyoxal (GO), and/or methylglyoxal (MGO) with several proteins, including ribonuclease A [EC 3.1.4.22] and its derivatives, alpha-chymotrypsin [EC 3.4.21.1], trypsin [EC 3.4.21.4], lysozyme [EC 3.2.1.17], pepsin [EC 3.4.23.1], rennin [EC 3.4.23.4], thermolysin, and insulin and its B chain, have been examined. From analyses of the reaction products, PGO was shown to be the most specific for arginine residues. GO and MGO also reacted rapidly with arginine residues, but they also reacted with lysine residues to a significant extent. A side reaction with N-terminal alpha-amino groups was observed with each of these reagents. 2. Two arginine residues out of four in ribonuclease A, two out of three in alpha-chymotrypsin, one out of two in trypsin, one out of two in pepsin, and one out of five in rennin appeared to react with PGO fairly rapidly, indicating a difference in the relative accessibility of these residues by the reagent. Extensive modification of the arginine residues by PGO occurred with RCM-derivatives of ribonuclease A and insulin B chain. The N-terminal isoleucine residues of alpha-chymotrypsin and trypsin appeared to be unreactive with PGO because of salt bridge formation with an aspartyl residue. The activity of alpha-chymotrypsin toward N-benzoyl-L-tyrosine ethyl ester and the lytic activity of lysozyme were lost rapidly on treatment with PGO, as in the case of ribonuclease A. Pepsin and rennin were only partially inactivated by reaction with PGO.
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PMID:Further studies on the reactions of phenylglyoxal and related reagents with proteins. 32 41

1. Digestion of procollagen I which trypsin, pepsin or pronase performed at 20 degrees C causes the release of acidic non-collagenous fragments and hydroxyproline-rich fraction. Enzymatic proteolysis performed at 41 degrees C (above the temperature of denaturation) results in degradation of procollagen I to low-molecular peptides. 2. The hydroxyproline-rich fraction obtained by limited proteolysis of procollagen I with pepsin (at 20 degrees C) contains a material corresponding to alpha and beta subunits of tropocollagen. Reduction of the hydroxyproline-rich fraction released by trypsin or pronase (at 20 degrees C) causes the appearance of polypeptides similar to pro-alpha subunits.
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PMID:Proteolysis of procollagen I. 32 74

One of the basic indicators specifying the quality of food products in general and culinary ones in particular is the extent of their assimilation in the gastrointestinal tract. Three culinary portions (sirloin, the outer part of the hind leg and the streak) of the beef of the Urals varieties horned cattle (black-mottled and Tagil) were investigated by the method of pepsin and trypsin digestion. The meat was analysed in the raw, cooked and fried state. The progress of the proteins proteolysis was controlled with reference to the tyrosine accretion. The raw meat was found to undergo digestion at a rather slow rate. The sirloin gets hydrolysed better than the other culinary portions. The meat of the Tagil variety is digested significantly in a more complete fashion than do the corresponding culinary parts of the black-mottle cattle. After heat treatment of the meat in all cases is demonstrable a material acceleration of the proteins proteolysis process, frying yielding a higher degree of splitting the meat proteins by comparison with cooking. Of the culinary portions under study it is the sirloin that shows the highest rate of digestion in its culinarily treated form, the outer part of the hind leg and the streak coming next. The fried and cooked meat of the most culinary portions of the Tagil variety undergo a more complete hydrolysis by comparison with black-mottled cattle meat. All this justifies recommending the meat of the Tagil variety horned cattle for obtaining the highest quality culinary products.
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PMID:[Digestion of raw and culinarily treated meat from cattle of Ural breeds]. 33 78

The ability of macrophage subpopulations, separated by virtue of differences in size, to liberate soluble factors able to reconstitute antibody and cell-mediated immune responses in macrophage-depleted lymphoid cultures has been investigated. Evidence is presented to show that all macrophages release trypsin- and pepsin-sensitive molecules with molecular weights of 30,000 to 35,000 and 50,000 to 70,000 that are able to reconstitute only syngeneic lymphocyte responses. In contrast, a molecule(s) with molecular weight of 10,000 to 15,000 daltons is released only by large macrophages and can apparently reconstitute both syngeneic and allogeneic lymphocyte responses. This material is also pepsin-sensitive and, to a lesser degree, trypsin-sensitive.
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PMID:Role of macrophage-derived factors in generation of cytotoxic and antibody responses. 33 50


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