Kodentsova V M, Petushkova E V, Tretyakova S S, Sokolova N I, Shabarova Z A
Biochem Int. 1985 Feb;10(2):195-203.
Affinity modification of HMM has been performed, using mixed anhydrides of AMP, epsilon AMP, ADP or IMP and sterically hindered aromatic carbonic acids. The affinity labelling site of HMM was demonstrated to be highly specific towards the adenosine fragment of the affinity analog. The number of phosphate groups and the hydrophobicity of the aromatic acid substitutents did not influence the mode of the analogs interaction with HMM. The data obtained confirms our previous suggestion that the nucleotide analogs in question modify the substrate binding site which is other than the active site of the enzyme.
已使用AMP、ε-AMP、ADP或IMP的混合酸酐以及位阻芳香族碳酸对重链肌球蛋白（HMM）进行了亲和修饰。结果表明，HMM的亲和标记位点对亲和类似物的腺苷片段具有高度特异性。磷酸基团的数量和芳香酸取代基的疏水性并不影响类似物与HMM的相互作用模式。所得数据证实了我们之前的推测，即所讨论的核苷酸类似物修饰的是酶活性位点之外的底物结合位点。
