Abstract
Cellular membranes were isolated from hypocotyls of Phaseolus aureus by continuous sucrose gradient centrifugation. Membrane fractions were used to study the subcellular localization of mannosyl transfer reactions that involved GDP-mannose as the mannosyl donor. The highest specific activity of the enzyme responsible for transfer of the mannosyl moiety to dolichyl monophosphate was found in the fraction enriched in membranes of the endoplasmic reticulum. In contrast, the highest specific activity of enzymes capable of incorporating mannose into ethanol-insoluble polymer, or possibly the highest concentration of endogenous mannosyl acceptors, was located in the fraction enriched in membranes of the Golgi apparatus.
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