Occurrence of GalNAcbeta1-4GlcNAc unit in N-glycan of royal jelly glycoprotein.
Elsewhere, we characterized the structure of twelve N-glycans purified from royal jelly glycoproteins (Kimura, Y. et al., Biosci. Biotechnol. Biochem., 64, 2109-2120 (2000)). Structural analysis showed that the typical high-mannose type structure (Man9-4GlcNAc2) accounts for about 72% of total N-glycans, a biantennary-type structure (GlcNAc2Man3GlcNAc2) about 8%, and a hybrid-type structure (GlcNAc1Man4GlcNAc2) about 3%. During structural analysis of minor N-glycans of royal jelly glycoproteins, we found that one had an N-acetyl-galactosaminyl residue at the non reducing end; most of such residues have been found in N-glycans of mammalian glycoproteins. By exoglycosidase digestion, methylation analysis, ion-spray (IS)-MS analysis, and 1H NMR spectroscopy, we identified the structure of the N-glycan containing GalNAc as; GlcNAc(beta)1-2Man(alpha)1-6(GalNAcbeta1 - 4GIcNAcbeta1 - 2Man(alpha)1 - 3)Manbeta1 - 4GlcNAc(beta)1-4GlcNAc. This result suggested that a beta1-4 GalNAc transferase is present in hypopharyngeal and mandibular glands of honeybees.
Kimura
Mariko
M
Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, Japan.
Hama
Yoichiro
Y
Tsumura
Kazunori
K
Okihara
Kiyoshi
K
Sugimoto
Hiroyuki
H
Yamada
Hideo
H
Kimurai
Yoshinobu
Y
D000818:Animals; D001516:Bees / Q000737:chemistry* / Q000201:enzymology; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D005227:Fatty Acids / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D007301:Insect Hormones / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000032:analysis* / Q000737:chemistry*; D000099219:Royal Jelly
D005227:Fatty Acids; D006023:Glycoproteins; D007301:Insect Hormones; D019476:Insect Proteins; D011134:Polysaccharides; D000099219:Royal Jelly