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PURIFICATION OF ALKALINE-PHOSPHATASE FROM THE INTESTINAL CONTENT OF COMMON SEAL (PHOCA-VITULINA-LARGA) BY IMMUNOAFFINITY CHROMATOGRAPHYстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Автор: SAKHAROV IY
- Журнал: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
- Том: 99
- Номер: 3
- Год издания: 1991
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 509
- Последняя страница: 511
- DOI: 10.1016/0305-0491(91)90330-G
- Аннотация: 1. A monoclonal antibody APP. 1 against harp seal alkaline phosphatase has been prepared. It was found that the antibody was cross-reacted with the intestinal alkaline phosphatase of common seal Phoca vitulina larga. 2. Purified antibody was linked to Sepharose 4B and used for immunoaffinity chromatographic purification of alkaline phosphatase from the intestinal content of common seal. A spec. act. of the purified enzyme was 7300 units per mg of protein. 3. The enzyme in 7.5% polyacrylamide gel in the presence of 2-mercaptoethanol and SDS was migrated as a single band of M(r) 67,000. The value of the apparent K(m) for common seal alkaline phosphatase was equal to 3.7 mM.
- Добавил в систему: Сахаров Иван Юрьевич