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Free access | 10.1172/JCI107008

Glycosyltransferases in human blood: I. Galactosyltransferase in human serum and erythrocyte membranes

Young S. Kim, Jose Perdomo, and James S. Whitehead

Gastrointestinal Research Laboratory, Veterans Administration Hospital, San Francisco, California 94121

Department of Medicine, University of California School of Medicine, San Francisco, California 94122

Find articles by Kim, Y. in: PubMed | Google Scholar

Gastrointestinal Research Laboratory, Veterans Administration Hospital, San Francisco, California 94121

Department of Medicine, University of California School of Medicine, San Francisco, California 94122

Find articles by Perdomo, J. in: PubMed | Google Scholar

Gastrointestinal Research Laboratory, Veterans Administration Hospital, San Francisco, California 94121

Department of Medicine, University of California School of Medicine, San Francisco, California 94122

Find articles by Whitehead, J. in: PubMed | Google Scholar

Published August 1, 1972 - More info

Published in Volume 51, Issue 8 on August 1, 1972
J Clin Invest. 1972;51(8):2024–2032. https://doi.org/10.1172/JCI107008.
© 1972 The American Society for Clinical Investigation
Published August 1, 1972 - Version history
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Abstract

Human serum and hemoglobin-free erythrocyte membranes were found to contain a galactosyltransferase which catalyzes the transfer of galactose from UDP-galactose to specific large and small molecular weight acceptors. The requirements for enzyme activity were found to be similar for the enzymes from both sources. However, the membrane-bound enzyme depended on a detergent for maximal activity. Mn++ was an absolute requirement for transfer and uridine nucleoside phosphates were inhibitors. The most effective acceptor for galactose was a glycoprotein containing N-acetylglucosamine residues in the terminal position of its oligosaccharide side chains, N-acetylglucosamine was also an acceptor. While the presence of α-lactalbumin in the incubation medium resulted in a significant decrease in the transfer of galactose to N-acetylglucosamine, glucose, which was not an acceptor for galactose in the absence of α-lactalbumin, became an excellent acceptor. The serum enzyme catalyzed the transfer of 54 nmoles of galactose per milliliter of serum per hour and its apparent Km for UDP-galactose was 7.5 × 10-6M. The membrane enzyme had a similar apparent Km. Using a quantitative assay system the enzyme was found to be present in all individuals studied, regardless of their blood type, secretor status, or sex.

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