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Susceptibility of bovine osteopontin to chymosin
Title: | Susceptibility of bovine osteopontin to chymosin |
Authors: | Kumura, Haruto1 Browse this author →KAKEN DB | Miura, Atsushi Browse this author | Sato, Eriko Browse this author | Tanaka, Tetsuya Browse this author | Shimazaki, Kei-ichi Browse this author |
Authors(alt): | 玖村, 朗人1 |
Issue Date: | Nov-2004 |
Publisher: | Cambridge University Press |
Journal Title: | Journal of Dairy Research |
Volume: | 71 |
Issue: | 4 |
Start Page: | 500 |
End Page: | 504 |
Publisher DOI: | 10.1017/S0022029904000391 |
Abstract: | Osteopontin (OPN) is an acidic phosphorylated glycoprotein found in many tissues and physiological fluids. Bovine OPN is a mature protein comprising 262 amino acids with a calculated molecular weight of 29 kDa. However, SDS-PAGE analysis reveals that the protein isolated from milk migrates to a molecular mass of 60 kDa (Sørensen & Petersen, 1993; Bayless et al. 1997). Bovine milk OPN is phosphorylated at 27 serine residues and one threonine residue (Sorensen et al. 1995); three O-glycosylated threonines were also identified, but no asparagine residues were glycosylated in spite of the presence of three putative N-glycosylation sites. In contrast, eight phosphates are recognized in bovine bone OPN (Salih et al. 1996), and 12 phosphoserines and one phosphothreonine are proposed in addition to five O-linked oligosaccharides and at most one N-linked oligosaccharide in the case of rat bone OPN (Prince et al. 1987). Thus, the possibility of tissue or species-specific differences in post-translational modification has been discussed. |
Rights: | Copyright © 2004 Cambridge University Press |
Type: | article |
URI: | http://hdl.handle.net/2115/5724 |
Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 玖村 朗人
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