Abstract
Summary The salt-extractable proteins from embryos of Helianthus annuus L. were separated into albumins (20%) and globulins (80%). Each fraction was analysed by pore-gradient electrophoresis. The predominant globulin, helianthin, has a molecular weight estimated to be 270,000 daltons. SDS-disc gel electrophoresis revealed two major pairs of disulphide-linked polypeptide subunits: I, 59,000 = 37,000 + 22,000 daltons, and II, 51,000 = 29,000 + 22,000 daltons. The data suggest that these linked polypeptide pairs associate non-covalently in the ratio 2:3 (I:II respectively).
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