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蚕豆11S球蛋白中间亚基的物理化学性质

Physicochemical properties of intermediary subunits of broad bean 11S globulin.

作者信息

Zheng B A, Matsumura Y, Mori T

机构信息

Research Institute for Food Science, Kyoto University, Uji, Kyoto, Japan.

出版信息

Phytochemistry. 1993 Jul;33(5):989-94. doi: 10.1016/0031-9422(93)85009-g.

DOI:10.1016/0031-9422(93)85009-g
PMID:7764032
Abstract

Three intermediary subunits of legumin, IS-I, IS-II and IS-III, were isolated. They were characterized by means of electrophoresis, amino acid and NH2-terminal sequence analyses. Reconstitution of pseudolegumin was carried out and the yield of 11S-size product from either IS-II or IS-III was more than 95%, while IS-I almost formed a 9S-size product and a small amount of 11S-size product. The pseudolegumins were similar to the native legumin in terms of their secondary structure. The products from IS-I and IS-II formed a stronger gel than the native legumin upon heating, but that from IS-III failed to form a self-supporting gel. IS-I plays an important role in increasing the gel hardness of legumin.

摘要

分离出豆球蛋白的三个中间亚基,即IS-I、IS-II和IS-III。通过电泳、氨基酸和氨基末端序列分析对它们进行了表征。进行了假豆球蛋白的重组,从IS-II或IS-III得到的11S大小产物的产率超过95%,而IS-I几乎形成了9S大小的产物和少量11S大小的产物。假豆球蛋白在二级结构方面与天然豆球蛋白相似。加热后,来自IS-I和IS-II的产物比天然豆球蛋白形成更强的凝胶,但来自IS-III的产物未能形成自支撑凝胶。IS-I在提高豆球蛋白的凝胶硬度方面起重要作用。

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