MODIFICATION TOLERABILITY OF THE HYPERVARIABLE REGION OF SOYBEAN PROGLYCININ

被引：20

作者：

KATSUBE, T ^{[1
]}

GIDAMIS, AB ^{[1
]}

KANAMORI, J ^{[1
]}

KANG, IJ ^{[1
]}

UTSUMI, S ^{[1
]}

KITO, M ^{[1
]}

机构：

[1] KYOTO UNIV,FOOD SCI RES INST,UJI,KYOTO 611,JAPAN

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1994年 / 42卷 / 11期

关键词：

CRYSTALLIZATION; GLYCININ; PROGLYCININ; PROTEIN ENGINEERING; SOYBEAN;

D O I：

10.1021/jf00047a049

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Glycinin is one of two major storage proteins of soybean seeds. To investigate the modification tolerability of the hypervariable region of proglycinin A(1a)B(1b) subunit, chemical properties of the hypervariable region were changed by deleting a polyglutamic acid sequence in the hypervariable region and substituting it with polylysine, polyglutamine, and polymethionine sequences. All modified proglycinins were overproduced in Escherichia coli cells, accumulated as soluble proteins, and self-assembled into trimers such as native proglycinin. This indicates that the hypervariable region can tolerate all modifications attempted in this study. Modified proglycinins purified to near homogeneity were attempted for crystallization. Although all of the modified proglycinins were partially limited-proteolyzed in the hypervariable regions, they could form crystals consisting of the two proglycinin molecular species: intact and limited-proteolyzed. Results suggest that the hypervariable region of proglycinin forms a flexible structure. It is concluded that this flexible structure may be responsible for the modification tolerability of the hypervariable region.

引用

页码：2639 / 2645

页数：7

共 38 条

[1] STRUCTURAL SIMILARITY BETWEEN LEGUMIN AND VICILIN STORAGE PROTEINS FROM LEGUMES [J].