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Isolation and Partial Characterization of Heat-denatured Products of Soybean 11S Globulin and Their Analysis by Electrophoresis
Authors:Tatsunori Yamagishi  Fumio Yamauchi  Kazuo Shibasaki
Institution:Department of Food Chemistry, Faculty of Agriculture, Tohoku University. Sendai 980, Japan
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.
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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