SURFACE-TOPOGRAPHY OF HISTIDINE-RESIDUES IN LYSOZYMES

被引：42

作者：

ZHAO, YJ

SULKOWSKI, E

PORATH, J

机构：

[1] ROSWELL PK CANC INST,DEPT MOLEC & CELLULAR BIOL,ELM & CARLTON ST,BUFFALO,NY 14263

[2] BIOCHEM SEPARAT CTR,UPPSALA,SWEDEN

[3] CHINESE ACAD SCI,INST MICROBIOL,BEIJING,PEOPLES R CHINA

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 202卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1991.tb16478.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several avian and mammalian c-type lysozymes were chromatographed on chelated (to iminodiacetate) and immobilized transition metal ions (Co2+, Ni2+, Cu2+ and Zn2+) under a variety of experimental conditions. The varied affinity of evolutionary variants of the lysozyme family for chelated metal ions, IDA-M(II), can be rationalized primarily in terms of the presence, multiplicity and microenvironments of histidine residues. The chromatographic resolution of some of these closely related proteins attests to the analytical power of immobilized metal-ion affinity chromatography.

引用

页码：1115 / 1119

页数：5

共 18 条

[1] REFINEMENT OF HUMAN LYSOZYME AT 1.5 A RESOLUTION ANALYSIS OF NONBONDED AND HYDROGEN-BOND INTERACTIONS [J].