N-Glycan structures of an osteopontin from human bone.
N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail. Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine. The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns. Two major N-glycan structures were also confirmed by mass spectrometry. The proposed structures are shown below. The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
Masuda
K
K
Suntory Institute for Bioorganic Research, Wakayama-dai, Shimamoto-cho, Mishima-gun, Osaka, 618, Japan.
Takahashi
N
N
Tsukamoto
Y
Y
Honma
H
H
Kohri
K
K
D000631:Aminopyridines; D001842:Bone and Bones / Q000737:chemistry*; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D053495:Osteopontin; D011134:Polysaccharides / Q000737:chemistry*; D012795:Sialoglycoproteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014018:Tissue Distribution
D000631:Aminopyridines; D011134:Polysaccharides; C506895:SPP1 protein, human; D012795:Sialoglycoproteins; D053495:Osteopontin; C032439:alpha-aminopyridine