Activation of F1 ‐ATPase isolated from potato tuber mitochondria

FEBS Letters

Andersson, B.¹  Glaser, E.¹  Norling, B.¹  Hamasur, B.¹ 

[1] Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden

关键词: F1-ATPase;    Anion activation;    Detergent activation;    Cooperativity;    (Plant mitochondrion);    F1;    F0;    catalytic respectively H+-translocating coupling factor of H+-ATPase;    Mops;    3-(N-morpholine)propanesulfonic acid;   

DOI  :  10.1016/0014-5793(87)80309-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ATP-hydrolyzing activity of F₁-ATPase purified from potato tubers mitochondria was stimulated 2- and 3.5-fold by anions, chloride and bicarbonate, respectively, and 5.5- and 6.5-fold by detergents, octyl glucoside and lauryl dimethylamine oxide (LDAO), respectively. The maximal specific activity of the activated F₁, 129 μmol/min per mg protein is the highest activity of plant mitochondrial F₁ hitherto reported and exceeds several-fold values reported earlier. In the absence of activators F₁-catalyzed ATP hydrolysis exhibits non-linear double-reciprocal plots of [ATP]⁻¹ vs v ⁻¹ indicative of negative cooperativity, while in the presence of activators, linear plots are observed. It is suggested that the activators reduce the cooperativity originating from the interaction between different subunits of the enzyme.

【 授权许可】

Unknown