Structural analyses of sugar chains from ricin A-chain variant.
Two glycopeptides were isolated from a tryptic digest of ricin A-chain variant by gel filtration and reversed-phase HPLC. Their amino acid compositions and sequences showed that Asn-10 and Asn-236 are glycosylated. The sugar chains were liberated from these glycopeptides by hydrazynolysis, N-acetylated, and pyridylaminated. Component analysis and comparison of elution positions of the purified pyridylamino (PA-) sugar chains with those of authentic PA-sugar chains from the major ricin A-chain by reversed-phase HPLC and size fractionation HPLC suggested that both sugar chains linked to Asn-10 and Asn-236 of the ricin A-chain variant are M3FX, identical to that linked to Asn-10 of the major ricin A-chain.
Kimura
Y
Y
Laboratory of Biochemistry, Faculty of Agriculture, Okayama University, Japan.
Kusuoku
H
H
Tada
M
M
Takagi
S
S
Funatsu
G
G
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D014644:Genetic Variation; D006020:Glycopeptides / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D012276:Ricin / Q000235:genetics / Q000302:isolation & purification; D014357:Trypsin
D006020:Glycopeptides; D010446:Peptide Fragments; D012276:Ricin; D014357:Trypsin