Abstract

Free and membrane-bound polyribosomes were isolated in an undegraded form from developing maize kernels. Translation of the membrane-bound polyribosomes in vitro produced one main radioactive protein. This protein was soluble in 70% ethanol and had the same mobility in electrophoresis on sodium dodecyl sulfate-gels as a zein standard. The ratio of [ 14C] leucine to [ 14C] lysine incorporated into the 70% ethanol extractable protein was similar to the mole fraction ratio of these amino acids in zein. The zein-like protein may represent as much as 50% of the total protein synthesized by the membrane-bound polyribosomes.

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