RAPID PURIFICATION OF MALATE SYNTHASE FROM COTYLEDONS OF BRASSICA-NAPUS L

A rapid and efficient method for the purifcation of malate synthase, a n enzyme uniquely confined to glyoxysomes, from cotyledons of Brassica napus L. has been developed. The two step purification procedure is b ased on the consequent utilization of the tendency of malate synthase to form high molecular weight aggregates. Malate synthase was purified 75-fold to apparent homogeneity with a specific activity of 180 nkat/ mg protein. The estimated molecular weight of malate synthase subunits was 63 kDa. Polyclonal antibodies raised against malate synthase in r abbits detect on Western blots only one single polypeptide with an ide ntical molecular weight.