A HEAT-STABLE ALKALINE-PHOSPHATASE FROM PENAEUS-JAPONICUS BATE (CRUSTACEA, DECAPODA) - A PHOSPHATIDYLINOSITOL-GLYCAN ANCHORED MEMBRANE-PROTEIN

被引：19

作者：

CHUANG, NN

机构：

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

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 95卷 / 01期

关键词：

D O I：

10.1016/0305-0491(90)90265-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. A heat-stable alkaline phosphatase was purified from Penaeus japonicus, with a final specific activity of 21,280 U/mg of protein. 2. 2. In polyacrylamide-gel electrophoresis under non-denaturing conditions, the purified shrimp alkaline phosphatase was found to ahve an identical molecular size and surface charge as the human placental enzyme. 3. 3. By using SDS-PAGE, the monomers of shrimp alkaline phosphatase were discovered to have a Mr 55,000 but those of human placental enzyme with a Mr 70,000. Deglycosylation decrease the Mr values of the subunits to 33,000 for shrimp alkaline phosphatase. 4. 4. The purified alkaline phosphatase from shrimp was recovered with both the attachment sites for sialic acids and phosphatidylinositol. 5. 5. The shrimp alkaline phosphatase has an isoelectric point (pI) of 7.6 and the human placental enzyme has a pI of 4.8. © 1989.

引用

页码：165 / 169

页数：5

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