PURIFICATION AND SOME PROPERTIES OF ALKALINE-PHOSPHATASE FROM THE HEPATOPANCREAS OF THE SHRIMP PENAEUS-JAPONICUS (CRUSTACEA, DECAPODA)

被引：31

作者：

CHUANG, NN

SHIH, SL

机构：

[1] Division of Biochemistry and Molecular Science, Institute of Zoology, Academia Sinica, Taipei, Nankang

来源：

JOURNAL OF EXPERIMENTAL ZOOLOGY | 1990年 / 256卷 / 01期

关键词：

D O I：

10.1002/jez.1402560102

中图分类号：

Q95 [动物学];

学科分类号：

071002 ;

摘要：

Alkaline phosphatase purified from the hepatopancreas of Penaeus japonicus is stable to heating at 65°C for 5 min. The specific activity of the purified enzyme is 25,000 units/mg of protein. After polyacrylamide gel electrophoresis under denaturing conditions, the purified alkaline phosphatase from shrimp was found to consist of deglycosylated monomers of Mr 40,000 and to retain the attachment sites for both sialic acid and phosphatidylinositol. The alkaline phosphatase from shrimp has an isoelectric point (pI) of 7.6 and becomes more alkaline after the removal of either sialic acid or phosphatidylinositol residues. Copyright © 1990 Wiley‐Liss, Inc., A Wiley Company

引用

页码：1 / 7

页数：7

共 28 条

[1] THE PREPARATION OF MONOCLONAL-ANTIBODIES TO HUMAN-BONE AND LIVER ALKALINE-PHOSPHATASE AND THEIR USE IN IMMUNOAFFINITY PURIFICATION AND IN STUDYING THESE ENZYMES WHEN PRESENT IN SERUM [J].