PMID: 6404553Feb 16, 1983Paper

13C-n.m.r.-spectral study of galactosyltransferase specificity with regard to the carbohydrate side-chain of native ovalbumin

Carbohydrate Research
E Berman, T L James

Abstract

As a prelude to studies using bovine N-acetylglucosaminide-beta-(1 leads to 4)-galactosyltransferase to label membrane-surface glycoproteins with isotopically enriched D-galactose, the structural specificity of the enzymic reaction with water-soluble, hen ovalbumin has been examined. The enzyme-catalyzed transfer of D-galactose from UDP-D-galactose requires a (nonreducing) terminal 2-acetamido-2-deoxy-D-glucosyl group and exhibits selectivity towards saccharide chains containing D-mannose. This study considers the structural specificity of the enzyme with regard to the anomeric linkage between 2-acetamido-2-deoxy-D-glucose and D-mannose in the carbohydrate chains of hen ovalbumin. Uniformly 13C-enriched D-galactose was enzymically attached to the ovalbumin carbohydrate chain (which exhibits microheterogeneity in its structure), the protein was hydrolyzed, and separate glycopeptide fractions were chromatographically isolated. The 13C-n.m.r. spectra (60.5 MHz) of the fractions revealed two peaks for the anomeric carbon atom of D-galactose. The two peaks, at 104.20 and 104.39 p.p.m., were ascribed to D-galactosyl groups attached to 2-acetamido-2-deoxy-D-glucose respectively linked beta-(1 leads to 4) and beta-(1 leads to 2), to D-...Continue Reading

References

Jul 15, 1976·European Journal of Biochemistry·J P PrieelsN Sharon
Aug 25, 2012·Investigative Ophthalmology & Visual Science·Shahina PardhanSusana T L Chung

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