Crystallization and Preliminary X-Ray Analysis of Soybean Proglycinins Modified by Protein Engineering
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概要
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Glycinin is one of the most abundant storage proteins in soybean seeds. We earlier reported the preparation of proglycinins modified by protein engineering to improve food functions. Crystals of the modified proglycinins (ΔI, ΔV8, IV + 4Met, V + 4Met, Gly12, and Ser88) expressed in Escherichia coli were grown, each under different suitable crystallization conditions. The crystals of ΔI, V + 4Met, Gly12, and Ser88 diffracted X-rays sufficiently for crystallographic analysis. ΔI, Gly12, and Ser88 crystals were tetragonal, space group P4_1 or P4_3, and with unit cell dimensions a = b = 114.3-l15.9Å and c = 145.1-146.1Å. V + 4Met crystals were monoclinic, space group P2, and with unit cell dimensions a = 118. 7Å, b = 78.1Å, c = 109.9Å, and β = 119°. The number of protomers per asymmetric unit of all of the crystals of these four modified proglycinins was about 3. This value is consistent with proglycinins being trimers. These data indicated that most of the modified proglycinin crystals examined here could be studied by X-ray crystallography to elucidate the relationships between the structure and the functional properties of glycinin at molecular level.
- 社団法人日本農芸化学会の論文
- 1994-04-23
著者
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Mikami Bunzo
Research Institute For Food Science Kyoto University
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KITO Makoto
Research Institute for Food Science, Kyoto University
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UTSUMI Shigeru
Research Institute for Food Science, Kyoto University
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KATSUBE Tomoyuki
Research Institute for Food Science, Kyoto University
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Katsube Tomoyuki
Research Institute For Food Science Kyoto University
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Gidamis B.
Research Institute for Food Science, Kyoto University
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Utsumi S
Division Of Agronomy And Horticultural Science Graduate School Of Agriculture Kyoto University
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Utsumi Shigeru
Research Institute For Food Science Kyoto University
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Kito M
Food Science Research Institute Fuji Oil Co. Ltd.
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Kito Makoto
Research Institute For Food Science Kyoto University
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Gidamis B.
Research Institute For Food Science Kyoto University
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