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- W4230597040 abstract "This chapter focuses on an extracellular protein called bone sialoprotein (BSP) that is expressed at high levels by osteoblasts at the sites of de novo bone formations. The protein has a restricted tissue distribution, essentially found only in bones and mineralized connective tissues. The molecule binds tightly to hydroxyapatite and appears to form an integral part of the mineralized matrix. BSP is composed of a single polypeptide chain. Its primary sequence reveals a paucity of hydrophobic residues, which predicts an open and flexible structure. BSP is isolated from bone matrix as a component of approximate molecular weight 60,000, containing both O- and N-linked oligosaccharides that are rich in sialic acid. The molecule is extensively glycosylated, about half of its serine residues are phosphorylated, and it contains the extended sequences of acidic amino acid residues. The chapter presents the primary structure, isolation methods, gene structure, and information on the structural and functional sites of BSP." @default.
- W4230597040 created "2022-05-11" @default.
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- W4230597040 date "1998-01-01" @default.
- W4230597040 modified "2023-09-24" @default.
- W4230597040 title "Bone sialoprotein BSP, bone sialoprotein II, BSPII" @default.
- W4230597040 doi "https://doi.org/10.1016/b978-012068911-8/50102-0" @default.
- W4230597040 hasPublicationYear "1998" @default.
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