Incorporation of N-Acetyl-d-glucosamine into Glycoproteins
作者： Irving R. Johnston , Edward J. McGuire , George W. Jourdian , Saul Roseman
DOI: 10.1016/S0021-9258(18)96406-9
关键词: Mannose 、 Sialidase 、 Glycoprotein 、 Enzyme 、 Hexosaminidase 、 Uridine diphosphate 、 Fetuin 、 Chemistry 、 Orosomucoid 、 Biochemistry
摘要: Abstract Fractionation of goat colostrum gave a 100- to 200-fold purified enzyme that catalyzed the transfer N-acetylglucosamine from uridine diphosphate certain glycoprotein acceptors. The latter were prepared α1-acid (orosomucoid) and fetuin by treatment with sialidase, β-galactosidase, hexosaminidase. Ribonuclease B ovalbumin active as acceptors without pretreatment glycosidases. Based on structures acceptors, it is tentatively concluded residue transferred terminal mannose units in glycoproteins. This reaction suggested be an important step biosynthesis
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