Heterogeneity in an isolated membrane protein Has the ‘authentic cytochrome oxidase’ been identified?

FEBS Letters

Babcock, Gerald T.⁵  Scott, Robert A.⁶  Chan, Sunney I.³  Hartzell, Charles R.¹  Palmert, Graham⁴  Beinert, Helmut² 

[1] Department of Research, Alfred I. DuPont Institute, Wilmington, DE 19899, USA;Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA;Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125, USA;Department of Biochemistry, William Marsh Rice University, PO Box 1892, Houston, TX 77251 USA;Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA;Departments of Chemistry and Biochemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA

关键词: X-ray absorption spectroscopy;    EPR;    Cyanide reactivity;    EXAFS;    extended X-ray absorption fine structure;    EPR;    electron paramagnetic resonance;   

DOI  :  10.1016/0014-5793(88)80273-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The criteria of homogeneity or native state of a protein are prone to become ambiguous when applied to membrane proteins, such as cytochrome-c oxidase, which are purified by extraction with detergents. Properties of the purified material depend on the detergent used and on details of the purification protocol followed with any single batch of a preparation. We present arguments to show that the evidence presently available in published form does not justify the designation [(1987) J. Biol. Chem. 262 3160–3164] of one type of preparation as being closer to the native state than others.

【 授权许可】

Unknown