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Susceptibility of bovine osteopontin to chymosin

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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
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)

Submitter: 玖村 朗人

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