Isolation and Partial Characterization of Heat-denatured Products of Soybean 11S Globulin and Their Analysis by Electrophoresis |
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Authors: | Tatsunori Yamagishi Fumio Yamauchi Kazuo Shibasaki |
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Institution: | Department of Food Chemistry, Faculty of Agriculture, Tohoku University. Sendai 980, Japan |
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Abstract: | Heat denaturation of soybean 11S globulin was examined at 70° and 100°C in phosphate buffer (pH 7.6), at 0.01 and 0.5 ionic strength. Gel electrophoresis (Davis system) indicated that heat-denatured soybean 11S globulin contained two major components (buffer-soluble form). But they were not identified at 70°C-0.5 ionic strength. Gel filtration followed by SDS-gel electrophoresis showed that the major components were composed of a monomer and at least three of kinds of oligomers containing only an acidic subunit. Gel filtration of the precipitate formed at 100°C at 0.5 ionic strength gave two peaks. SDS-gel electrophoresis indicated that the first peak contained aggregates of highly polymerized subunits, and the second peak contained a monomer of basic subunit and seven kinds of oligomers with various proportions of basic subunits to an acidic subunit. |
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Keywords: | small ubiquitin-related modifier (SUMO) SUMO-activating enzyme (SUMO-E1) baculovirus-insect cell system protein expression post-translational protein modification |
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