Modulation of cytochrome oxidase kinetics by indirect antibody action

FEBS Letters

Cooper, C.E.¹  Nicholls, P.¹ 

[1] Department of Biological Sciences, Brock University, St. Catharines, Ontario L2S 3A1, Canada

关键词: Cytochrome oxidase;    Subunit V;    Cytochrome c;    Substrate binding;    Antibody;    Enzyme inhibition;   

DOI  :  10.1016/0014-5793(89)80775-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Polyclonal antibodies raised against isolated subunit V from beef heart cytochrome oxidase or against the intact enzyme increase its apparent affinity for the substrate cytochrome c at the high-affinity site while diminishing the turnover at that site. At the low-affinity site the major action of both types of antibody is to reduce the apparent affinity for cytochrome c. At high ionic strengths the kinetic effect of anti-subunit V is very small although it still binds to the enzyme. The results are interpreted in terms of a model for the enzyme in which antibodies can modulate cytochrome oxidase kinetics by affecting the binding of cytochrome c, even if the antibody-binding site is on a subunit not directly involved in substrate binding.

【 授权许可】

Unknown