Structure determination of the carbohydrate chains of rat alpha-fetoprotein.
By affinity chromatography on concanavalin A (ConA) linked to Sepharose, S-carboxymethylated rat alpha-fetoprotein could be separated into two molecular variants: a ConA-reactive and a ConA-nonreactive fraction. The carbohydrate chains were quantitatively released from the protein by hydrazinolysis. Based on methylation analysis and high-resolution 1H-NMR spectroscopy of the re-N-acetylated hydrazinolysates, the carbohydrate structures of the two ConA-molecular variants of alpha-fetoprotein were established. The ConA-reactive species contains two N-glycosidic carbohydrate units per molecule, both having the following structure: (formula; see text) The ConA-nonreactive species possesses also two N-glycosidically linked oligosaccharide chains per molecule; each of these has the following structure: (formula; see text)
D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002855:Chromatography, Thin Layer; D003208:Concanavalin A; D005260:Female; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D009844:Oligosaccharides / Q000032:analysis; D011247:Pregnancy; D051381:Rats; D011919:Rats, Inbred Strains; D000509:alpha-Fetoproteins
D002241:Carbohydrates; D009844:Oligosaccharides; D000509:alpha-Fetoproteins; D003208:Concanavalin A