利用单克隆抗体分离与人合体滋养层细胞膜相关的胎盘型碱性磷酸酶。

Isolation of placental-type alkaline phosphatase associated with human syncytiotrophoblast membranes using monoclonal antibodies.

作者信息

Webb P D, McLaughlin P J, Risk J M, Johnson P M

出版信息

Placenta. 1986 Sep-Oct;7(5):405-15. doi: 10.1016/s0143-4004(86)80028-5.

DOI:10.1016/s0143-4004(86)80028-5

Abstract

Placental-type alkaline phosphatase (PLAP) has been purified from human term syncytiotrophoblast microvillous plasma membranes by immunoaffinity chromatography using the immobilized monoclonal antibodies H317 and H315. The eluted enzymatically active PLAP had a molecular weight in the regions of 115K and 130K, with an occasional higher molecular weight form at 180K. On reduction to a 66K monomeric form, both enzymatic activity and immunoactivity against the PLAP-reactive monoclonal antibodies were lost. The monomeric form of syncytiotrophoblast microvillous plasma membrane- (StMPM-)associated PLAP displayed electrophoretic polymorphism on 2D-PAGE.

摘要

通过使用固定化单克隆抗体H317和H315的免疫亲和色谱法，已从人足月合体滋养层微绒毛质膜中纯化出胎盘型碱性磷酸酶（PLAP）。洗脱的具有酶活性的PLAP分子量在115K和130K范围内，偶尔会出现180K的更高分子量形式。还原为66K单体形式后，针对PLAP反应性单克隆抗体的酶活性和免疫活性均丧失。合体滋养层微绒毛质膜（StMPM）相关PLAP的单体形式在二维聚丙烯酰胺凝胶电泳（2D-PAGE）上显示出电泳多态性。

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