采用脱氨再生几丁质凝胶亲和层析从萝卜叶中获得了ＰＡＧＥ圆盘电泳均一的溶菌酶，并通过微量蒸发扩散法获得其结晶。用ｐＨ动力学研究方法和化学修饰法对该酶的活性中心进行了初步研究，实验结果表明：－ＣＯＯＨ（Ｇｌｕ／Ａｓｐ）基团、Ｔｒｐ及Ｈｉｓ残基可能为酶活性所必需。采用对Ｔｙｒ、Ｃｙｓ、Ａｒｇ、Ｓｅｒ／Ｔｈｒ残基专一的修饰剂对酶作用后，酶活性基本上不受影响。同时，酶活性受到组胺和ＧｌｃＮＡｃ抑制。讨论了萝卜溶菌酶与鸡蛋清溶菌酶和木瓜溶菌酶的活性中心的相互差异。 Uniformly purified PAGE electrophoresis of lysozyme was obtained from radish leaves by deamidation-regenerated chitin gel affinity chromatography and its crystallinity was obtained by micro-evaporative diffusion. The activity centers of this enzyme were studied by pH dynamic method and chemical modification method. The results showed that -COOH (Glu / Asp), Trp and His residues may be necessary for the enzyme activity. Enzymatic activity is essentially unaffected by the use of modifiers specific to Tyr, Cys, Arg, Ser / Thr residues. At the same time, enzyme activity is inhibited by histamine and GlcNAc. The interaction between radish lysozyme and egg white lysozyme and papaya lysozyme was discussed.