来自日本对虾（甲壳纲：十足目）的一种热稳定碱性磷酸酶：一种磷脂酰肌醇聚糖锚定膜蛋白。

A heat-stable alkaline phosphatase from Penaeus japonicus Bate (Crustacea: Decapoda): a phosphatidylinositol-glycan anchored membrane protein.

Chuang N N

Division of Biochemistry and Molecular Science, Institute of Zoology, Academia Sinica, Taipei, Taiwan, Republic of China.

Comp Biochem Physiol B. 1990;95(1):165-9. doi: 10.1016/0305-0491(90)90265-u.

Abstract

A heat-stable alkaline phosphatase was purified from Penaeus japonicus, with a final specific activity of 21,280 U/mg of protein. 2. In polyacrylamide-gel electrophoresis under non-denaturing conditions, the purified shrimp alkaline phosphatase was found to have an identical molecular size and surface charge as the human placental enzyme. 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 decreases the Mr values of the subunits to 33,000 for shrimp alkaline phosphatase. 4. The purified alkaline phosphatase from shrimp was recovered with both the attachment sites for sialic acids and phosphatidylinositol. 5. The shrimp alkaline phosphatase has an isoelectric point (pI) of 7.6 and the human placental enzyme has a pI of 4.8.

摘要

从日本对虾中纯化出一种热稳定碱性磷酸酶，最终比活性为21,280 U/mg蛋白质。2. 在非变性条件下的聚丙烯酰胺凝胶电泳中，发现纯化的虾碱性磷酸酶与人类胎盘酶具有相同的分子大小和表面电荷。3. 通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE），发现虾碱性磷酸酶的单体分子量为55,000，而人类胎盘酶的单体分子量为70,000。去糖基化使虾碱性磷酸酶亚基的分子量降至33,000。4. 从虾中纯化的碱性磷酸酶同时具有唾液酸和磷脂酰肌醇的附着位点。5. 虾碱性磷酸酶的等电点（pI）为7.6，人类胎盘酶的pI为4.8。