Structure of Glycinin and Its Significance in Thermal Polymerization of Glycinin Molecule
| Project/Area Number |
61560095
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
応用生物化学・栄養化学
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| Research Institution | Kyoto University |
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Principal Investigator |
MORI Tomohiko Research Institute for Food Science, Kyoto University, 食糧科学研究所, 助教授 (10027188)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUMURA Yasuki Research Instituti for Food Science, Kyoto University, 食糧科学研究所, 助手 (50181756)
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| Project Period (FY) |
1986 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1987: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1986: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Interaction of glycinin molecule / Structure and Functionality of glycinin / グリシニンの高分子化 / グリシニンのゲル化 |
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| Research Abstract |
lls globulin (referred to as glycinin), one of the major components of the soybean storage protein, is a multisubunit protein consisting of six subunits in which the acidic and basic polypeptides are linked by disulfide bridges in 1:1 ratio. The glycinin exhibits thermal gelling ability, i.e., polymerization of glycinin molecules. In this study, the correlation between the gelling ability and the protein structure of glycinin was investigated. (1) The constituent subunits of glycinin, ASI,ASII,ASIII, and ASIV, exhibited each characteristic contribution to interactions of glycinin molecules in the course of polymerization. (2) The nucleotide and deduced amino acid sequences of ASI (A_<la>B_x) subunit from G. max var. Shirotsurunoko were determined. The amino acid sequence was compared with those from var. CX635-1-1-1 and Bonminori. The comparison indicated that a considerable degree of homology exists among those subunits, and that homologous regions, variable regions and cysteine residues are located in specific regions of the polypeptide sequence similarly in all the subunits. (3) The interactions of glycinin molecules in the course of polymerization seemed to occur at specific regions of the surface of glycinin molecule through hydrophobic interactions and disulfide exchange reactions. The variable regions and free cysteine residues in polypeptide sequence may be involved in the hydrophobic interaction and disulfide exchange reaction, respectively.
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Report
(2 results)
Research Products
(15 results)
