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SUBSTRATE-SPECIFICITY OF COLLAGENOLYTIC PROTEASES FROM THE HEPATOPANCREAS OF THE KAMCHATKA CRABстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
- Авторы: SAKHAROV IY, LITVIN FE
- Журнал: Biochemistry (Moscow)
- Том: 57
- Номер: 1
- Год издания: 1992
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 44
- Последняя страница: 49
- Аннотация: The substrate specificity of two isoenzymes of the collagenolytic protease of the Kamchatka crab was studied Both proteases were shown to effectively hydrolyze types I and III collagen, as well as gelatin; the assortment of products formed as a result of enzymatic hydrolysis differs for isoenzymes A and C An investigation of the hydrolysis of a number of peptides showed that the crab isoenzyme A preferentially cleaves peptide bonds where the carbonyl constituents are Arg and Lys residues, whereas isoenzyme C prefers hydrophobic amino acids. The catalytic constants of the hydrolysis of a number of low-molecular-weight substrates in the presence of the crab proteases were determined which made it possible to classify the crab isoenzyme A as trypsinlike protease and isoenzyme C as a chymotrypsinlike protease. It was found that the peptide substrates of collagenase Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala are not digested by isoenzymes of the Kamchatka crab collagenolytic protease.
- Добавил в систему: Сахаров Иван Юрьевич