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Abstract
A Golgi apparatus-rich fraction isolated from rat liver catalyzes the transfer of glucosamine from UDP-N-acetylglucosamine to endogenous protein acceptors. The Golgi-associated transfer accounts for almost half of the total activity of the original homogenate. Plasma membrane and endoplasmic reticulum fractions are practically devoid of activity. GDP-mannose and GTP stimulate this transfer, possibly by sparing UDP-N-acetylglucosamine from enzymatic hydrolysis. UDP-glucose, UDP-galactose, UTP, UDP, and UMP are inhibitory. Digestion with pronase converts the radioactive product of this transfer into a trichloroacetic acid-soluble form. All of the radioactive material cochromatographs with glucosamine, following acid hydrolysis of pronase glycopeptides.
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