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Sulphate is a competitive inhibitor of the binding of nucleotide to myosin A comparison with phosphate
Author(s) -
Tesi Chiara,
Barman Thomas,
Travers Franck
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80326-0
Subject(s) - myosin , phosphate , nucleotide , chemistry , biophysics , biochemistry , inorganic phosphate , ionic bonding , binding site , ion , biology , organic chemistry , gene
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.