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http://dx.doi.org/10.5187/JAST.2003.45.3.491

Purification and Properties of Osteopontin from Bovine Milk  

Choi, K.W. (Department of Food and Life Science, Sungkyunkwan University)
Kim, D.W. (National Livestock Research Institute, RDA)
Lee, S.W. (Department of Food and Life Science, Sungkyunkwan University)
Publication Information
Journal of Animal Science and Technology / v.45, no.3, 2003 , pp. 491-498 More about this Journal
Abstract
The purpose of this study is to observe purification and properties of osteopontin(OPN) from bovine milk. The purification of osteopontin from bovine milk was performed by using ion-exchange and hydrophobic chromatography. SDS-PAGE analysis revealed that the protein migrated at Mw. 60,000. NH2-terminal sequence analysis of the first seven amio acids revealed the protein to be identical to that previously reported for bovine OPN. 35-wk-old chickens, including 3 Single Comb White Leghorn (SCWL), were used to produce egg yolk antibody(IgY) against OPNas a antigen. However, the anti-OPN antibody activities determined by ELISA. Immunological assy of OPN in milk was performed using radial immunodiffusion test based on the standard curve of pure OPN. The radial precipitation lines of four different milk samples indicated that the concentrations of OPN in the milk samples were within the range of 31.7 to 39.7${\mu}g$/ml. On inhibition with OPN on precipitation of calcium phosphate, OPN was slightly higher than casein phosphopeptide(CPP) and poly-glutamic acid.
Keywords
Osteopontin; Anti-OPN; Radial immunodiffusion; CPP; Calcium phosphate;
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