骨桥蛋白
糖基化
苏氨酸
糖蛋白
化学
生物化学
天冬酰胺
牛乳
丝氨酸
残留物(化学)
分子质量
磷酸化
氨基酸
分子生物学
生物
酶
免疫学
作者
Haruto Kumura,Atsushi Miura,Eriko Sato,Tetsuya Tanaka,K. Shimazaki
出处
期刊:Journal of Dairy Research
[Cambridge University Press]
日期:2004-11-01
卷期号:71 (4): 500-504
被引量:8
标识
DOI:10.1017/s0022029904000391
摘要
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.
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