【摘要】 采用再生几丁质亲和层析和两性电解质等电聚焦电泳，纯化了扁豆荚几了酶，其分子量３０ｋＤ，等电点为９．１，主要呈内切酶活性。扁豆荚中不同组织几丁酶比活力有很大差异。在豆荚发育过程中，其酶活性变化呈单峰曲线，而比活力则持续上升，表明扁豆几丁酶活性变化与发育相关。经ＨｇＣｌ２处理后，扁豆荚壳和种子的几丁酶活性均明显提高。在扁豆荚发育的不同阶段，几丁酶的诱导特性也有明显差异，幼嫩豆荚几丁酶诱导活性的增加更为明显。更多还原

【Abstract】 Chitinase (EC 3. 2. 1. 14) was purified from the hulls of hyacinth peapods by affinity chromatography on acolumn of regenerated chitin and by isoelectric focusing. The purified chitinasegave a single protein band on sodiumdodecyl sulfate polyacrylamide gel electrophoresis with a molecular weight of30 kD (Fig. 5 ). The enzyme wasproved to be endochitinase and the isoelectric point (pl) was PH 9. 1 (Fig.4 ). The specific activity of the chitinase in the hulls of hyacinth pea podswas about 17 times as high as that inthe cotyledons and I I times that in theembryo (Table 1 ). The specific activityof chitinase in the hull increased withdevelopment and maturation of thepods. The time course of the change ofchitinase activity had a single peak onthe 13th day after anthesis (Fig. 1 ).The results indicate that chitinase activity is in relationship with development.The chitinase activity in the hulls and inthe seeds of the pods treated with HgCI,was higher than in those of untreatedones. The chitinase activity increase induced by HgCl2 was larger in immaturepods than in mature ones(Fig. 3 ).更多还原