Catalytic properties of the ATPase on submitochondrial particles after exchange of tightly bound nucleotides under different steady state conditions

FEBS Letters

Boyer, Paul D.¹  Myers, Jill A.¹ 

[1] Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, CA 90024, USA

关键词: ATPase;    control;    Oxygen exchange;    Mitochondria;    Bound nucleotide;    SMP;    submitochondrial particles;    PEP;    phosphoenolpyruvate;    S-13;    5-chloro-3-t-butyl-2′-chloro-4′-nitrosalicylanilide;    EDTA;    ethylenediamine—tetraacetic acid;    HEPES;    4-(2-hydroxy-ethyl)-1-piperazine—ethanesulfonic acid;    ATPase;    mitochondrial proton-translocating adenosine triphosphatase (often called F1-ATPase);   

DOI  :  10.1016/0014-5793(83)80771-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Energized submitochondrial particles were subjected to high or low [³H]ATP/[³H]ADP ratios, maintained during steady state by a pyruvate kinase or hexokinase regenerating system, respectively. Under both steady state conditions, about 1.4 mol [³H]nucleotide/mol ATPase was retained but considerably more [³H]ATP was retained with the high [³H]ATP/[³H]ADP ratio. The ATPase activity and the oxygen exchange of these differentially labeled SMP were the same, suggesting a lack of control function of non-catalytic tightly bound nucleotides.

【 授权许可】

Unknown