| Literature DB >> 3402615 |
Abstract
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 epsilon-ATP and ATP to myosin. At low ionic strengths, the Ki 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 epsilon-ATP to actomyosin.Entities:
Mesh：
Substances：
Year: 1988 PMID： 3402615 DOI： 10.1016/0014-5793(88)80326-0
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124