Chstiakova L A, Cherkasov I A, Kravchenko N A
Biokhimiia. 1978 Jul;43(7):1167-74.
Hen egg-white lysozyme (EC 3.2.1.17) was carboxymethylated with iodoacetic acid and the individual products of various degree of modification were isolated by column chromatography on Amberlite CG-50. Peptide mapping of the products obtained reveals that His-15, Lys-1, -33, -96 (or -97) residues are blocked; the Lys-13 and -116 residues are unmodified. Salt activation of the carboxymethylated derivatives is facilitated with the increase of the number of modified groups; this fact is consistent with the increased lytic activity and affinity to substrate of the derivatives at lowered ionic strength.
用碘乙酸对鸡蛋清溶菌酶（EC 3.2.1.17）进行羧甲基化处理，并通过在Amberlite CG - 50上进行柱色谱分离不同修饰程度的各个产物。对所得产物的肽图谱分析表明，组氨酸-15、赖氨酸-1、-33、-96（或-97）残基被封闭；赖氨酸-13和-116残基未被修饰。随着修饰基团数量的增加，羧甲基化衍生物的盐激活作用增强；这一事实与衍生物在较低离子强度下裂解活性和对底物亲和力的增加相一致。
