Subunit structure of γ-conglycinin in soybean seeds |
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Authors: | F. Yamauchi W. Sato Y. Kamata |
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Affiliation: | Department of Food Chemistry, Faculty of Agriculture, Tohoku University, Sendai 980, Japan |
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Abstract: | Dissociated subunits of purified γ-conglycinin were isolated on a DEAE-Sephadex A-50 column. A single band was seen on two kinds of gel electrophoresis and isoleucine was shown as the only N-terminal amino acid. The isolated subunit reacted with antisera to the native γ-conglycinin. The Mr of the subunit was 51 000–51 500 estimated by urea-acetic acid and SDS-urea gel electrophoresis. A value of 50 000 was obtained by gel filtration with guanidine-hydrochloric acid on Sepharose CL-6B. The γ-conglycinin molecule was found to be made up of three subunits. This was determined by cross-linking the subunits and then submitting them to gel electrophoresis. Differences and similarities of subunit structure among γ-conglycinin, β-conglycinin and glycinin are discussed. |
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Keywords: | Leguminosae soybean protein subunit structure electrophoresis γ-conglycinin. |
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