从牛胰腺中纯化激肽释放酶原。

Purification of prokallikrein from bovine pancreas.

作者信息

al-Hamidi A A, Bailey G S

机构信息

Department of Chemistry and Biological Chemistry, University of Essex, Colchester, U.K.

出版信息

Biochim Biophys Acta. 1991 Sep 2;1075(1):88-92. doi: 10.1016/0304-4165(91)90079-v.

DOI:10.1016/0304-4165(91)90079-v

PMID:1892869

Abstract

A prokallikrein was isolated from bovine pancreas by a multi-step procedure involving gel filtration, hydrophobic interaction and anion-exchange chromatographies. The purification was initially monitored by measurement of the kinin-releasing activity of the activated zymogen. Later, when the pure prokallikrein had been isolated, a specific radioimmunoassay for the zymogen was set up and that was employed to provide estimates of 323-fold and 28% for the overall degree of purification and percentage recovery of prokallikrein. The relative molecular weight of prokallikrein was found to be 26,900 by SDS gel electrophoresis and its isoelectric point was established as pH 4.55.

摘要

通过包括凝胶过滤、疏水相互作用和阴离子交换色谱在内的多步程序，从牛胰腺中分离出一种前激肽释放酶。最初通过测量活化酶原的激肽释放活性来监测纯化过程。后来，当分离出纯的前激肽释放酶时，建立了针对该酶原的特异性放射免疫测定法，并用于估计前激肽释放酶的总体纯化程度为323倍，回收率为28%。通过SDS凝胶电泳发现前激肽释放酶的相对分子质量为26,900，其等电点确定为pH 4.55。