Kodentsova V M, Petushkova E V, Drutsa V L, Tret'iakova S S
Biokhimiia. 1982 Jul;47(7):1193-7.
Using mixed anhydride of AMP and mesitylene carboxylic acid carrying a fluorescent or radioactive label, it was found that the previously established irreversible inhibition of myosin ATPase is a result of protein covalent binding to the nucleotide residue of the inhibitor. The stoichiometry of the affinity labelling of heavy meromyosin is 1 mole of nucleotide residue of mixed anhydride per 1 mole of protein, that of subfragment 1-0.5 mole per 1 mole of protein. The lack of irreversible inhibition of the ATPase activity of subfragment 1 is suggestive of an existence of a regulatory substrate-binding site in the myosin molecule.
使用携带荧光或放射性标记的AMP与均三甲苯羧酸的混合酸酐，发现先前确定的肌球蛋白ATP酶的不可逆抑制是蛋白质与抑制剂的核苷酸残基共价结合的结果。重酶解肌球蛋白亲和标记的化学计量为每1摩尔蛋白质1摩尔混合酸酐的核苷酸残基，亚片段1的化学计量为每1摩尔蛋白质0.5摩尔。亚片段1的ATP酶活性缺乏不可逆抑制表明肌球蛋白分子中存在一个调节性底物结合位点。
