THE HYDROPHOBIC DOMAIN OF PENICILLIN ACYLASE IS NEGATIVELY CHARGED

被引：8

作者：

KARYEKAR, SK ^{[1
]}

HEGDE, MV ^{[1
]}

机构：

[1] UNIV POONA,DEPT CHEM,DIV BIOCHEM,POONA 411007,MAHARASHTRA,INDIA

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1991年 / 13卷 / 02期

关键词：

PENICILLIN ACYLASE; HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBIC DOMAIN;

D O I：

10.1016/0141-0229(91)90169-B

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];

摘要：

Difficulties in hydrophobic chromatography of penicillin acylase due to electrostatic charges have been overcome by modification of the phenyl sepharose matrix. Phenyl sepharose-diamines showed very strong binding and resulted in poorer recoveries of penicillin acylase, while phenyl sepharose-glycine, which has an ionized COO group, gave 94%-95% recovery. The results suggest the possible presence of a negative charge in the hydrophobic domain of penicillin acylase.

引用

页码：139 / 141

页数：3

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