LOCATION AND QUANTIFICATION OF METAL-IONS IN ENZYMES COMBINING POLYACRYLAMIDE-GEL ELECTROPHORESIS AND PARTICLE-INDUCED X-RAY-EMISSION

被引：22

作者：

SZOKEFALVINAGY, Z ^{[1
]}

BAGYINKA, C ^{[1
]}

DEMETER, I ^{[1
]}

KOVACS, KL ^{[1
]}

QUYNH, LH ^{[1
]}

机构：

[1] HUNGARIAN ACAD SCI,CTR BIOL RES,INST BIOPHYS,H-6701 SZEGED,HUNGARY

来源：

BIOLOGICAL TRACE ELEMENT RESEARCH | 1990年 / 26-7卷

关键词：

bacterial hydrogenase; metalloenzyme; metalloprotein; particle-induced X-ray emission; PIXE; polyacrylamide gel electrophoresis (PAGE); trace element analysis;

D O I：

10.1007/BF02992662

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：

A method is presented to identify and determine the relative amounts of protein-bound metal ions in situ. Proteins or their subunits are directly scanned by a collimated proton beam of 3 MeV energy, and the characteristic X-rays produced are detected. The determination of Fe content of an iron-sulfur protein (HiPiP), as well as the Fe and Ni analysis of the hydrogenese from Thiocapsa roseopersina, have shown the feasibility of this technique. © 1990 Humana Press Inc.

引用

页码：93 / 101

页数：9