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Your search keyword '"Monastyrnaia, M. M."' showing total 2 results
Start Over Author "Monastyrnaia, M. M." Topic trypsin inhibitors
2 results on '"Monastyrnaia, M. M."'

1. [Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases].

Author

Sokotun IN, Gnedenko OV, Leĭchenko EV, Monastyrnaia MM, Kozlovskaia EP, Mol'nar AA, and Ivanov AC

Subjects
Animals, Humans, Kinetics, Peptide Hydrolases metabolism, Protein Binding, Sea Anemones metabolism, Trypsin Inhibitors isolation & purification, Trypsin Inhibitors metabolism, Peptide Hydrolases chemistry, Sea Anemones chemistry, Trypsin Inhibitors chemistry
Abstract

The interaction of inhibitor VJ (InhVJ), isolated from sea anemone R. macrodactylus, with different proteases was investigated. The following enzymes were tested: serine proteases (trypsin, alpha-chymotrypsin, plasmin, thrombin, kallikrein), cysteine protease (papain) and aspartic protease (pepsin). Inhibitor VJ interacted only with trypsin and 6-chymotrypsin. Kinetic and thermodynamics parameters of intermolecular complexes formation were determined: KD = 7,38 x 10(-8) M and 9,93 x 10(-7) M for pairs InhVJ/trypsin and InhVJ/alpha-chymotrypsin, respectively.

Published
2006

2. [Low-molecular cytolysins and trypsin inhibitors from sea anemone Radianthus macrodactylus. Isolation and partial characterization].

Author

Zykova TA, Monastyrnaia MM, Apalikova OV, Shvets TV, and Kozlovskaia EP

Subjects
Amino Acids analysis, Animals, Brachyura, Chromatography, Affinity, Chromatography, Gel, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Cytotoxins analysis, Cytotoxins toxicity, Electrophoresis, Polyacrylamide Gel, Glycine, Hemolysis, Histamine Antagonists analysis, Histamine Antagonists isolation & purification, Histamine Antagonists pharmacology, Histamine Antagonists toxicity, Isoelectric Focusing, Male, Mice, Molecular Weight, Rats, Sphingomyelins pharmacology, Trypsin Inhibitors analysis, Cytotoxins isolation & purification, Cytotoxins pharmacology, Sea Anemones chemistry, Trypsin Inhibitors isolation & purification, Trypsin Inhibitors pharmacology
Abstract

Two low-molecular cytolytic toxins (RmI and RmII) and four trypsin inhibitors were isolated from the aqueous extract of sea anemone Radianthus macrodactylus. The method of isolation involved precipitation with acetone, gel filtration on acrylex P-4, ion-exchange chromatography on CM-32 cellulose, affinity chromatography on trypsin-binding sepharose 4B, ion exchange chromatography on an Ultrapore TSK CM-3SW column, and reversed phase HPLC on a Silasorb C18 column. RmI, RmII, and JnI inhibitor displayed molecular masses 5100, 6100, and 7100 Da, respectively, when subjected to SDS-PAGE. The isoelectric points were 9.2 and 9.3 for RmI and RmII, respectively. The amino acid composition and N-terminal amino acid residue (glycine) were determined for RmI, RmII, and JnI. Both proteins were nontoxic to mice and crabs. Hemolytic activity was determined to be 25 and 20 HU/mg for RmI and RmII, respectively, and their action on erythrocyte membrane was not inhibited by exogenous sphingomyelin. RmI and RmII exhibited antihistamine activity.

Published
1998

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