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)

The binding isotherms of native bovine serum albumin with cationic detergents, such as octyl, decyl, dodecyl and tetradecylpyridinium bromides were determined at pH 6.8 and 3.4 at 25 degrees C. The isotherms for dodecyl and tetradecylpyridinium bromides were also determined at 3 degrees C. The average number of detergent cations bound increased with increasing hydrocarbon chain length. At low detergent concentration the binding of all alkylpyridinium bromides was smaller at pH 3.4 than at pH 6.8. Dodecylpyridinium bromide was bound to native beta-lactoglobulin, aldolase, ovalbumin, haemoglobin, myoglobin, lysozyme, trypsin and ribonuclease at pH 6.8. No binding occurred to alpha-chymotrypsin and chymotrypsinogen. The free enthalpy change, --delta G degrees, calculated from intrinsic association constants K was determined.
Acta Biochim Pol 1979
PMID:Protein-cationic detergent interaction. Equilibrium dialysis study of the interaction of bovine serum albumin and other proteins with alkylpyridinium bromide. 49 43

Porcine elastase II (EC 3.4.21.-), a pancreatic proteinase with elastolytic activity, hydrolyses the oxidized beta-chain of insulin with major cleavages occurring at Leu17-Val18, Phe24-Phe25, Phe25-Tyr26 and Tyr26-Thr27. Canine leucocytic elastase splits the same substrate with major sites at Val12-Glu13 and Val18-Cys19 O3H. This indicates similarity of elastase II to chymotrypsins (EC 3.4.21.1 or 3.4.21.2) and of dog leucocyte enzyme to human granulocyte elastase and porcine pancreatic elastase I (EC 3.4.21.11).
Acta Biochim Pol 1979
PMID:Specificity of elastases: degradation of the oxidized beta-chain of insulin by porcine pancreatic elastase II and dog leucocyte elastase. 49 46

Commercial nisin was fractionated using a Bio-Gel P-10 column and ion-exchange chromatography on CM-sephadex C-25. Pure nisin having a titre of 40 X 10(6) units per gram was obtained. In polyacrylamide-gel electrophoresis the pure nisin gave three bands. It is suggested that heterogeneity of nisin is due to the presence of several biological polypeptides. The pure nisin is digested by chymotrypsin but it is not affected by TPCK-trypsin and pepsin.
Acta Microbiol Pol A 1976
PMID:The use of gel-filtration for the isolation of pure nisin from commercial products. 82 Jan 64

1. Susceptibility to inhibitors of neutral protease from calf thymus chromatin has been compared with that of trypsin. The chromatin protease reacts stoichiometrically with the inhibitors specific for trypsin (diisopropylfluorophosphate, tosyl-lysyl chloromethane, soybean trypsin inhibitor and Kunitz basic inhibitor from pancreas), but not with the inhibitor specific for chymotrypsin (tosyl-phenylalanyl chloromethane). 2. Chromatin protease, similarly as trypsin, cleaves Lys-X and Arg-X peptide bonds. 3. It is concluded that the structure of active site region of both enzymes is very similar.
Acta Biochim Pol 1976
PMID:Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin. 98 80

It has been shown that keratinase--proteinase PIV, the main enzyme of the proteolytic system of S. fradiae, is characterized by high effectiveness in its action on AcAla3OMe--exceeding elastase in catalytic effectiveness several times. This proteinase also cleaves ester and amide bonds formed by the residues of aromatic and basic amino acids, but with a lower effectiveness than chymotrypsin or trypsin. It has also been shown that proteinase IV is a typical serine enzyme highly sensitive to DFP, acting in strongly alkaline pH (about 11.2), with molecular weight 24 kDa and does not contain cysteine.
Acta Microbiol Pol 1992
PMID:Proteinases of Streptomyces fradiae. III. Catalytic and some physico- chemical properties of keratinolytic proteinase. 128 46

The effect of new CCK receptor antagonist, lorglumid on taurocholate AEP in rats was studied. Lorglumid was applied intraperitoneally at a dose of 5.6 mg/kg BW immediately after taurocholate injection into choledochopancreatic duct. Activity of amylase, antithrombin III (AT III), alpha 1 protease inhibitor (alpha 1 PI), alpha 2 antiplasmin (alpha 2 AP) and alpha 2 M) in plasma, trypsin and chymotrypsin in pancreata were measured after 1, 3, 6 h of AEP. In AEP treated by lorglumid serum amylase activity and pancreatic wet weight was significantly reduced. The use of lorglumid prevented the increase of alpha 1 PI and alpha 2 AP compared to not treated animals. AT III and alpha 2 M in plasma and trypsin and chymotrypsin activity in pancreata did not change significantly in all groups. The mortality of the lorglumid treated rats was significantly lower in comparison with control group. It is concluded that lorglumid in taurocholate AEP moderates the changed plasma proteinase-antiproteinase balance. Our results indicate a protective effect of lorglumid in this model of acute experimental pancreatitis.
Mater Med Pol
PMID:The effect of a cholecystokinin receptor antagonist lorglumid on the proteinase-antiproteinase balance in taurocholate acute experimental pancreatitis (AEP) in rats. 130 47

The 39-kDa DNA polymerase beta (beta-Pol) molecule can be readily converted into two constituent domains by mild proteolysis; these domains are represented in an 8-kDa N-terminal fragment and a 31-kDa C-terminal fragment [Kumar et al. (1990a) J. Biol. Chem. 265, 2124-2131]. Intact beta-Pol is a sequence-nonspecific nucleic acid-interactive protein that binds both double-stranded (ds) and single-stranded (ss) polynucleotides. These two activities appear to be contributed by separate portions of the enzyme, since the 31-kDa domain binds ds DNA but not ss DNA, and conversely, the 8-kDa domain binds ss DNA but not ds DNA [Casas-Finet et al. (1991) J. Biol. Chem. 266, 19618-19625]. Truncation of the 31-kDa domain at the N-terminus with chymotrypsin, to produce a 27-kDa fragment (residues 140-334), eliminated all DNA-binding activity. This suggested that the ds DNA-binding capacity of the 31-kDa domain may be carried in the N-terminal segment of the 31-kDa domain. We used CNBr to prepare a 16-kDa fragment (residues 18-154) that spans the ss DNA-binding region of the 8-kDa domain along with the N-terminal portion of the 31-kDa domain. The purified 16-kDa fragment was found to have both ss and ds polynucleotide-binding capacity. Thermodynamic binding properties for these activities are similar to those of the intact enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Mammalian DNA polymerase beta: characterization of a 16-kDa transdomain fragment containing the nucleic acid-binding activities of the native enzyme. 142 Jan 47

The fiber proteins of adenovirus serotype 2 Ad2 and serotype 3 Ad3 and structural protein IIIa of wild type Ad2 and Ad2 ts 112 mutant were cloned and expressed in E. coli. For the expression of both fiber proteins a gene expression system based on bacteriophage T7 RNA polymerase was used. The expressed proteins constituted 1-3% of total host cell protein. Both proteins were insoluble and inclusion bodies were observed. The proteins could be purified from cellular debris by extraction with 6 M urea followed by chromatography in the presence of diminishing concentration of urea. The folding of recombinant fiber proteins was assessed by sensitivity to proteases and gel filtration. Both proteins were synthetized as trimers. Ad2 recombinant fiber has a much less compact structure than native Ad2 fiber, since on gel filtration it is excluded before the native fiber. It is also much more sensitive to chymotrypsin digestion than the native protein. Contrary to that, Ad3 recombinant fiber is much less sensitive to proteolytic cleavage and on gel filtration has the same exclusion volume as the trimeric native fiber of Ad3.
Acta Biochim Pol 1990
PMID:Structural proteins of adenovirus. Expression in Escherichia coli. 208 15

Ethanol and in higher degree acetaldehyde displayed inhibitory effect directed against amidolytic activity of trypsin and chymotrypsin. The decrease of the activity of both enzymes is related to the concentration of these compounds. The rate of inhibition of amidolytic activity of chymotrypsin with both reagents is more evident in comparison to trypsin.
Mater Med Pol
PMID:Inhibitory effect of ethanol and acetaldehyde on the amidolytic activity of trypsin and chymotrypsin. 249 Dec 74

Two trypsin inhibitors, CPPTI-I and CPPTI-II of Mr 3 250 and 7 850, respectively, were isolated from resting white bush seeds. Both inhibitors are cysteine-rich proteins. In addition to trypsin, they inhibit a trypsin-like enzyme isolated from Streptomyces griseus proteinase but they do not act on chymotrypsin, kallikrein or subtilopeptidase A. The isolated inhibitors contain a lysine residue in position P1 of the reactive site.
Acta Biochim Pol 1985
PMID:Isolation of two trypsin inhibitors from resting seeds of the white bush (Cucurbita pepo var. patissonina) and their properties. 393 88


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