Masuda K, Takahashi N, Tsukamoto Y, Honma H, Kohri K
Suntory Institute for Bioorganic Research, Wakayama-dai, Shimamoto-cho, Mishima-gun, Osaka, 618, Japan.
Biochem Biophys Res Commun. 2000 Feb 24;268(3):814-7. doi: 10.1006/bbrc.2000.2224.
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.).
