ELASTASE FROM HEPATOPANCREAS OF THE KING CRAB (PARALITHODES CAMTSCHATICA)статья
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:1053
Последняя страница:1060
Аннотация:A homogeneous preparation of elastase from the king crab Paralithodes camtschatica hepatopancreas with specific activity 3.7 units per mg protein toward Boc-(Ala)(3)-pNA was isolated by ion-exchange chromatography on DEAE-Sepharose and gelfiltration on Sephacryl S-200. The molecular weight and isoelectric point of the king crab elastase are 28.5 kD and 4.5, respectively The amino acid composition of the elastase was determined The enzyme exhibits its maximal catalytic activity at pH 8.0-8.5, the values of K-m and k(cat) toward Suc-(Ala)(3)-pNA being 4 mM and 3 sec(-1), respectively. In contrast to N-ethylmaleimide, 2-mercaptoethanol, p-chloromercuribenzoate, EDTA, and o-phenanthroline, elastinal and diisopropyl fluorophosphate completely suppress the protease activity, suggesting that the enzyme is a member of the family of serine elastases. Activation of the king crab elastase by inorganic salts was found The enzyme is rather stable in neutral and basic solutions and in the presence of surfactants at temperatures below 45 degrees C (pH 8.0).