Identification of different quaternary structures of beef heart cytochrome‐c oxidase by two‐dimensional polyacrylamide gel electrophoresis

FEBS Letters

Heinrichs, Marc¹  Schönert, Hansjürgen¹ 

[1] Institut für Physikalische Chemie, Abteilung für Biopolymere, RWTH Aachen, Templergraben 59, 5100 Aachen, FRG

关键词: Cytochrome-c oxidase;    Nondenaturing gradient polyacrylamide gel electrophoresis;    Nonionic detergent;    2D-PAGE;    native DGPAGE;    discontinuous gradient polyacrylamide gel electrophoresis under nondenaturing conditions;    SDS-DPAGE;    discontinuous SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(87)80300-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A two-dimensional gel electrophoresis is decribed to identify different quartemary structures of the heart cytochrome-c oxidase. Bovine enzyme was purified and separated by discontinuous gradient polyacrylamide gel electrophoresis under nondenaturing conditions in the 1st dimension into several discrete complexes and thereupon shown to be heterodisperse in Triton X-100 and dodecyl maltoside. A discontinuous SDS-polyacrylamide gel electrophoresis in the 2nd dimension was used to determine the subunit composition of the isolated complexes. One of these represents the intact enzyme with 12 different polypeptides while the others have an incomplete subunit composition.

【 授权许可】

Unknown