SUBUNIT STRUCTURE OF HALOPHILIC MALATE-DEHYDROGENASE FROM HALOARCULA-MARISMORTUI

被引：3

作者：

DANIEL, E

AZEM, A

SHAKED, I

MEVARECH, M

机构：

[1] TEL AVIV UNIV,GEORGE S WISE FAC LIFE SCI,DEPT MOLEC MICROBIOL & BIOTECHNOL,IL-69978 TEL AVIV,ISRAEL

[2] TEL AVIV UNIV,GEORGE S WISE FAC LIFE SCI,DEPT BIOCHEM,IL-69978 TEL AVIV,ISRAEL

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1993年 / 106卷 / 02期

关键词：

D O I：

10.1016/0305-0491(93)90320-5

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：

1. The subunit structure of halophilic malate dehydrogenase from Haloarcula marismortui was studied by the method of crosslinking with bifunctional reagent. 2. Exposure of the enzyme to glutardialdehyde followed by sodium dodecyl sulphate gel electrophoresis resulted in the appearance of four bands with mobilities corresponding to monomeric polypeptide chains and crosslinked polypeptide chain dimers, trimers and tetramers. 3. Our findings are not consistent with the currently accepted dimeric structure of the enzyme. They provide a strong indication that halophilic malate dehydrogenase is composed of four identical subunits.

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页码：401 / 405

页数：5

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