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- Title
Characteristics Of Oat (Avena sativa L.) Seed Globulins.
- Authors
BURGESS, S. R.; SHEWRY, P. R.; MATLASHEWSKI, G. J.; ALTOSAAR, I.; MIFLIN, B. J.
- Abstract
The major storage proteins of the oat grain are globulins. These have been extracted and characterized. Sucrose density gradient ultracentrifugation separated the globulins into three main fractions with sedimentation coefficients of about 3S, 7S and 12S, of which the latter was the major component. The 12S globulin, when analysed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE), was found to consist chiefly of proteins of about 55 000 molecular weight. This major protein was purified and when reduced gave rise to two classes of subunit. The larger subunits had molecular weights between 35 000 and 42 000 and isoelectric points between pH 5.0 and 7.0 whereas the smaller were between 19 000 and 25 000 molecular weight with isoelectric points of pH 8.0 to 9.0. The large subunits were poor in methionine and not all of them were cleaved by cyanogen bromide. In contrast to the 12S proteins, the migration on SDS-PAGE of the components of the 7S and 3S globulins was not affected by reduction. The major components of the 7S fraction were polypeptides of about 55 000 molecular weight. It is suggested from these results that the oat storage globulins have certain similarities to the globulins present in the seeds of legumes and other dicotyledonous plants.
- Publication
Journal of Experimental Botany, 1983, Vol 34, Issue 10, p1320
- ISSN
0022-0957
- Publication type
Article