N-Glycan structures of osteopontin (a bone matrix protein) from human bone
(lumbar vertabrate) are reported in detail, Asn-linked glycan portion was r
eleased from 100 mu g of osteopontin by digestion with glycoamidase A (from
sweet almond), and the reducing ends of the N-glycans were reductively ami
nated with 2-aminopyridine. The derivatized N-glycans were separated and st
ructurally identified by a multidimensional mapping technique on HPLC colum
ns. Two major N-glycan structures were also confirmed by mass spectrometry.
The proposed structures are shown below, The result should permit future c
omparison with the N-glycan structures of osteopontins obtained from other
sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
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(C) 2000 Academic Press.