Vaintraub I A, Bassüner R, Shutov A D
Nahrung. 1976;20(8-9):763-71. doi: 10.1002/food.19760200802.
The action of trypsin on the reserve proteins of the leguminous seeds belonging to Vicieae and Phaseoleae tribes was investicated. The hydrolysis of11S and 7S proteins of Vicieae proceeds relatively fast and some of the proteins are hydrolyzed practically completely. The hydrolysis of most of the investigated reserve proteins of the Phaseoleae tribe proceeds much slower, while that of 7S proteins of four Phaseolus species of American origin stops after the cleavage of only 10-20% of peptide bonds capable of reacting. Analogous results were obtained studying the action of chymotrypsin on a more restricted number of proteins. Both trypsin and chymotrypsin hydrolyze the same parts of Ph. vulgaris 7S protein, splitting off peptides which can be separated on a Sephadex G-50 column. The nonhydrolyzable high molecular weight core has a slightly smaller sedimentation coefficient and a higher elelctrophoretic mobility than the native protein and is able to dimerize at high ionic strength. Urea does not alter the hydrolyzability of the core butt the latter is partially hydrolyzed after the action of urea or guanidine hydrocholoride in the presence of mercaptoethanol.
研究了胰蛋白酶对属于巢菜族和菜豆族的豆科种子贮藏蛋白的作用。巢菜族11S和7S蛋白的水解进行得相对较快，一些蛋白几乎完全被水解。菜豆族大多数被研究的贮藏蛋白的水解要慢得多，而原产于美国的四种菜豆属植物的7S蛋白在仅裂解10 - 20%能够反应的肽键后水解就停止了。研究胰凝乳蛋白酶对数量较少的蛋白的作用也得到了类似结果。胰蛋白酶和胰凝乳蛋白酶都水解菜豆7S蛋白的相同部分，裂解出可在葡聚糖G - 50柱上分离的肽段。不可水解的高分子量核心部分的沉降系数略小于天然蛋白，电泳迁移率高于天然蛋白，并且在高离子强度下能够二聚化。尿素不会改变核心部分的可水解性，但在巯基乙醇存在下，尿素或盐酸胍作用后，核心部分会被部分水解。
