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野花生豆凝集素（ＣＭＬ）经ＳｅｐｈａｄｅｘＧ－２００测得分子量为１０３．ＯｋＤ．用对二甲基氨基苯甲醛（ＤＡＢ）为显色剂，测得每个ＣＭＬ分子含有５．９个色氨酸残基．在ｐＨ５．１，含８ｍｏｌ／Ｌ脲的醋酸缓冲液中，Ｎ－溴代丁二酰亚胺（ＮＢＳ）可修饰ＣＭＬ分子中的５．６个色氨酸（Ｔｒｐ）残基，同时使ＣＭＬ的凝血活性完全丧失．用焦碳酸二乙酯（ＤＥＰＣ）和Ｎ－乙酰顺丁烯酰胺（ＮＥＭ）分别修饰ＣＭＬ的组氨酸残基和半胱氨酸巯基后，ＣＭＬ的活性均无变化．ＣＭＬ在天然状态下荧光发射峰位于３３６ｎｍ处，用ＣＭＬ的专一性抑制糖Ｎ－乙酰半乳糖胺研究色氨酸的微环境，发现Ｎ－乙酰半乳糖胺可以淬灭ＣＭＬ中８８％的色氨酸残基萤光，Ｓｔｅｒｎ－Ｖｏｌｍｅｒ常数Ｋ＝１．７３Ｌ／ｍｏｌ．同时发现Ｎ－乙酰半乳糖胺能够保护ＣＭＬ，避免ＮＢＳ对ＣＭＬ的修饰作用，表明色氨酸可能是ＣＭＬ维待活性所必需，并直接参与和专一性抑制糖的结合，其微环境较为疏水．
Wild Peanut Lectin (CML) has a molecular weight of 103 measured by Sephadex G-200. OkD. With p-dimethylaminobenzaldehyde (DAB) as a chromogenic reagent, each CML molecule was found to contain 5.9 tryptophan residues. N-bromosuccinimide (NBS) modified 5.6 tryptophan (Trp) residues in CML molecules in pH5.1, 8 mol / L urea-containing acetate buffer, and CML The complete loss of coagulation activity. No change was observed in the activity of CML after modifying histidine residues and cysteine thiol groups with diethyl pyrocarbonate (DEPC) and N-acetyl maleimide (NEM). CML in the natural state fluorescence emission peak located at 336nm, CML with specific inhibition of sugar N-acetylgalactosamine tryptophan microenvironment and found N-acetylgalactosamine can quench CML 88% of the color Amino acid residue fluorescence, Stern-Volmer constant K = 1.73 L / mol. At the same time, it was found that N-acetylgalactosamine can protect CML and avoid the modification effect of NBS on CML, indicating that tryptophan may be necessary for the maintenance of CML and directly participate in and specifically inhibit the binding of sugar, and its microenvironment is relatively hydrophobic .