Abstract
A soluble glycosyltransferase which transfers N-acetylgalactosamine from UDP-N-acetylgalactosamine to exogenous protein acceptors is present in human serum. The proteins capable of accepting the hexosamine are basic myelin proteins from beef brain and spinal cord, and bovine submaxillary mucin from which sialic acid and hexosamine have been removed. Other proteins studied do not serve as acceptors. Alkaline borohydride treatment of the labeled protein acceptors releases over 80% of the radioactivity as N-acetylgalactosaminitol thus indicating that the galactosaminylation takes place primarily at the hydroxyaminoacids in these proteins. The enzyme is present in the sera of all individuals, irrespective of their ABO blood group. In this respect it differs from the galactosaminyl transferase that is presumed to be responsible for blood group A antigenicity.
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