PURIFICATION OF CARBOXYPEPTIDASE-B BY METAL CHELATION AFFINITY-CHROMATOGRAPHY

被引：18

作者：

MARQUEZMENDEZ, M ^{[1
]}

机构：

[1] UNIV TECHNOL COMPIEGNE,TECHNOL SEPERAT LAB,F-60206 COMPIEGNE,FRANCE

来源：

JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS | 1992年 / 24卷 / 1-2期

关键词：

CARBOXYPEPTIDASE; METAL CHELATE AFFINITY CHROMATOGRAPHY; HYDROPHOBIC INTERACTION;

D O I：

10.1016/0165-022X(92)90046-D

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Norwegian lobster carboxypeptidase B (CPB) was purified in one step using immobilized metal chelate affinity chromatography (IMAC). The separation is based on the property that CPB has a high affinity for metal ions such as Cu2+. The CPB was purified from an hepatopancreas extract containing several endo- and exo-proteolytic activities. Its homogeneity was demonstrated by SDS-electrophoresis and isoelectric focusing in immobilized pH gradients. The implication of hydrophobic interaction between this enzyme and the IDA-Cu2+ gel is postulated.

引用

页码：51 / 61

页数：11

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