Knorre D G, Buneva V N, Baram G I, Godovikova T S, Zarytova V F
FEBS Lett. 1986 Jan 1;194(1):64-8. doi: 10.1016/0014-5793(86)80052-7.
Affinity labelling of pancreatic RNase with 4-(N-2-chloroethyl-N-methylamino)benzylamide and (N----P) N-methylimidazolide of d(pTpA) results in the formation of monomodified enzyme derivatives retaining partially enzymatic activity. These data together with some cases described in the literature are considered as suggesting the dynamic nature of the enzyme-reagent complex represented by a set of states differing in the probability of intra-complex reaction. In particular, modification may proceed in a low probability state with an especially favorable mutual orientation of reagent and some protein residue remote from the active site of the enzyme resulting in the removal of the covalently attached reagent moiety from the active center.
用4-(N-2-氯乙基-N-甲基氨基)苄酰胺和d(pTpA)的(N----P)N-甲基咪唑鎓对胰腺核糖核酸酶进行亲和标记，结果形成了保留部分酶活性的单修饰酶衍生物。这些数据以及文献中描述的一些案例被认为表明了酶-试剂复合物的动态性质，该复合物由一组在复合物内反应概率上不同的状态所代表。特别是，修饰可能在低概率状态下进行，此时试剂与远离酶活性位点的一些蛋白质残基具有特别有利的相互取向，从而导致共价连接的试剂部分从活性中心去除。
