Abstract
The proteins from rape seed meal and serum albumin were incubated with the 35S-labelled glucosinolates progoitrin, gluconapin, and glucoalyssin in a variety of reaction conditions. Intact glucosinolates and oxazolidinethiones were found to combine with the proteins to a very small extent, independently of pH; but the isothiocyanates reacted readily with the proteins at pH values higher than 6. Fractionation of the rape seed protein conjugates on Sephadex G200 showed that isothiocyanates particularly reacted with the basic low molecular weight proteins. Changes in UV-spectrum and electrophoretic mobility after reaction with isothiocyanates were also demonstrated.
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