[Properties of trypsin and chymotrypsin in dioxan-water mixtures].
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Chemical Phenomena↗
Biomedical subjects
V V Mosolov
Publications and source records attributed to V V Mosolov.
[The effect of fatty acids and urea on the esterase activity and structure of trypsin].
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Chemical Phenomena↗
[Purification of Bacillus mesentericus proteolytic enzymes by affinity chromatography].
By means of affinity chromatography on Ovomucoid-Sepharose two proteinases hydrolyzing casein and elastin were isolated from the supernatant of the Bacillus mesentericus culture medium. The activity yield of proteinases was 100%. The characteristics of the purified enzymes were studied. It is demonstrated that B. mesentericus possesses several proteinases.
Bacillus↗
[Covalent immobilization of the pancreatic trypsin inhibitor on a polymeric carrier].
Covalent immobilization of the pancreatic trypsin inhibitor onto a polymeric carrier was accomplished by introducing a double C = C bond in the inhibitor with a subsequent copolymerization of the activized inhibitor with acrylamide and N,N'-methylenebisacrylamide. To prevent a loss of the antitryptic activity under acylation of lysine residues of the reactive centre, the inhibitor was preliminary bound to a complex with trypsin, which was destructed by acidifying the solution before copolymerization. The antitryptic activity of the immobilized inhibitor was shown to be equal to the activity of the inhibitor in the native state.
Acrylamide↗
[Purification of soybean trypsin inhibitor by an immunosorption method].
A technique for isolation of the trypsin inhibitor from soya beans (Kunitz inhibitor) was developed with affinity chromatography as a main step, the immobilized antibodies of the inhibitor being used as a sorbent. The inhibitor obtained was homogeneous according to the data of electrophoresis in PAAG and had the specific activity equal to that of an inhibitor preparation obtained by affinity chromatography on trypsin-sepharose.
Animals↗
[Antitryptic and antichymotryptic activity of salivary gland secretions and intestinal contents of the medical leech Hirudo medicinalis].
Antithrombin, antitryptic and antichymotryptic activities were studied in various tissues of medical leech Hirudo medicinalis. Maximal antithrombin and antitryptic activities were found in secretion products of salivary glands. Intestinal chyme exhibited distinct antichymotryptic activity. The antichymotrypsin activity correlated with antithrombin activity in hirudin preparations, obtained after isoelectrofocusing and free of bdellines. A preparation of "pseudohirudin" exhibited neither antitryptic nor antichymotryptic activities.
Animals↗
[Affinity chromatography of a cysteine proteinase inhibitor from chicken egg protein].
A method of affinity chromatography of the inhibitor of cysteine proteinases from chick egg protein using immobilized ficin has been developed. This method yields a highly active inhibitor in an essentially homogeneous state. The molecular weight of the inhibitor is 14,000. The inhibitor suppresses the activity of ficin and papain but produces no effect on the proteolytic activity of trypsin, chymotrypsin, Asp. oryzae serine proteinase or subtilisine. Isoelectric focusing of the inhibitor has revealed the major band with pI 4.35.
Animals↗
[Effect of protease inhibitors on influenza virus reproduction].
Natural inhibitors of proteases have been shown to inhibit plaque production by influenza virus. Investigation of the fate of viral intracellular proteins revealed the inhibiting effect of these inhibitors on their posttranslation cutting. It is assumed, therefore, that the antiviral effect of the preparation under study is associated with inhibition of viral proteins cutting, in particular, of hemagglutinin. A comparative study of the antiviral activity of inhibitors of proteases from various sources was carried out: from potato, haricot, common honey locust, as well as trypsin inhibitor from soybeans. The highest antiviral activity determined by the plaque reduction test was found with the preparation obtained from potato.
Animals↗
[An alcohol-soluble trypsin inhibitor from beans].
An ethanol soluble protein-trypsin inhibitor was isolated from kidney bean seeds. The inhibitor purification included gel chromatography of ethanol soluble proteins on Sephadex G-75 and affine chromatography on immobilized trypsin and chymotrypsin. The inhibitor suppressed activites of trypsin, chymotrypsin and in part trypsin-chymotrypsin activity of pronase but did not influence subtilizin. The inhibitor at a dose of 15-17.5 mug decreased by 50% the activity of 100 mug trypsin. By isoelectric focusing it was shown that the inhibitor isolated from kidney beans consisted of four isoinhibitors with pH of 4.3, 4.5, 4.7, and 4.9.
Chemical Phenomena↗