使用金属螯合亲和色谱法从大肠杆菌碱性磷酸酶中去除锌离子。

Use of metal chelate affinity chromatography for removal of zinc ions from alkaline phosphatase from Escherichia coli.

作者信息

Lubińska V K, Muszyńska G

机构信息

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.

出版信息

J Chromatogr. 1990 Nov 28;522:171-7. doi: 10.1016/0021-9673(90)85187-z.

DOI:10.1016/0021-9673(90)85187-z

PMID:2081752

Abstract

Alkaline phosphatase from Escherichia coli (APEC) is not retained at 4 degrees C on a metal-free tris(carboxymethyl)ethylenediamine (TED) column, but at 15 degrees C the metalloenzyme becomes bound to the gel. Chromatography of phosphatase on metal-free TED gel indicates a decline in its enzymic activity and zinc content to about 26% and 40%, respectively. The activity of chromatographed APEC can be partially restored by addition of zinc ions, indicating that metal-free TED gel is capable of removing zinc ions from alkaline phosphatase.

摘要

来自大肠杆菌的碱性磷酸酶（APEC）在无金属的三（羧甲基）乙二胺（TED）柱上于4℃时不会保留，但在15℃时金属酶会与凝胶结合。在无金属的TED凝胶上对磷酸酶进行色谱分析表明，其酶活性和锌含量分别下降至约26%和40%。通过添加锌离子可部分恢复经色谱分析的APEC的活性，这表明无金属的TED凝胶能够从碱性磷酸酶中去除锌离子。