人前列腺酸性磷酸酶：I. 分离

Human prostatic acid phosphatases: I. Isolation.

作者信息

Choe B K, Pontes E J, Bloink S, Rose N R

出版信息

Arch Androl. 1978 May;1(3):221-6. doi: 10.3109/01485017808988340.

DOI:10.3109/01485017808988340

PMID:83814

Abstract

A new purification procedure is described for the human prostatic acid phosphatase. The procedure included carboxy-methyl-Sephadex and Concanavalin A affinity column chromatography. The purified enzyme has a high specific enzyme activity and is free from any extraneous proteins judging from immunochemical criteria and biochemical criteria such as SDS-polyacrylamide gel electrophoresis. The purified enyzme produced a monospecific anti-PAP antisera in animals and this anti-PAP antibody did not cross-react with other human acid phosphatases.

摘要

本文描述了一种新的人前列腺酸性磷酸酶纯化方法。该方法包括羧甲基葡聚糖凝胶和伴刀豆球蛋白A亲和柱层析。从免疫化学标准和生化标准（如SDS-聚丙烯酰胺凝胶电泳）判断，纯化后的酶具有较高的比酶活性，且不含任何外源蛋白。纯化后的酶在动物体内产生了单特异性抗PAP抗血清，且该抗PAP抗体与其他人酸性磷酸酶无交叉反应。

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