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KMID : 0903519830260010065
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1983 Volume.26 No. 1 p.65 ~ p.72
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Fractionation and Electrophoretic Patterns of Rice Proteins
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Abstract
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The composition of four rice protein groups is greatly affected by the extraction conditions. The extraction amounts of albumins and glubulines primarily depended on the temperature rather than the method of extraction. The total amount of glutelins, the major components of rice storage proteins, could be extracted by a successive extraction processes, extraction with 0.5% SDS-0.1M borate buffer(pH 8.3) followed by extraction with 0.5% SDS-0.6% β-mercaptoethanol-0.1M borate buffer(pH 8.3). The extracted amounts of glutelin with these solvents were 54.1 and 45% respectively. The further purification of SDS soluble glutelins was achieved by Sephadex G-150 gel column chromatography.
The molecular weight of the components in four protein groups has been estimated by SDS-polyacrylamide gel electrophoresis with or without β-mercaptoethanol.
The comparison of albumins and globulins by starch gel electrophoresis at pH 3.1 permitted us to identify seven rice varieties. However, at pH 8.95, the specific bands for Japonica type rice varieties were observed.
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