What question did this study set out to answer?

To assess sulphate's ability to inhibit nucleotide binding to myosin compared to phosphate.

August 15, 1988

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

Key Points

To assess sulphate's ability to inhibit nucleotide binding to myosin compared to phosphate.
Utilized rapid reaction methods including rapid flow quench and stopped flow.
Measured inhibition at varying ionic strengths and conditions.
Analyzed binding effectiveness using epsilon-ATP and ATP.
Sulphate exhibited competitive inhibition of epsilon-ATP and ATP binding to myosin, with Ki in the micromolar range.
Sulphate was more effective than phosphate under multiple tested conditions.
Neither sulphate nor phosphate significantly inhibited epsilon-ATP binding to actomyosin.

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.

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

Key Points

Abstract

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