Sulphate is a competitive inhibitor of the binding of nucleotide to myosin A comparison with phosphate

FEBS Letters

Travers, Franck¹  Barman, Thomas¹  Tesi, Chiara¹ 

[1] INSERM U128, CNRS, BP 5051, 34033 Montpellier Cedex, France

关键词: Myosin;    Sulfate inhibition;    Reaction kinetics;    Cryoenzymology;    S1;    subfragment 1 of myosin;    ϵ-ATP;    1-N 6-etheno-ATP;   

DOI  :  10.1016/0014-5793(88)80326-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

By the use of rapid reaction methods (rapid flow quench and stopped flow) it has been shown that sulphate is a competitive inhibitor of the binding of ε-ATP and ATP to myosin. At low ionic strengths, the K _i was in the micromolar range. Under several conditions used sulphate was more effective than phosphate. Neither anion was very effective in inhibiting the binding of ε-ATP to actomyosin.

【 授权许可】

Unknown