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Semi-preparative isolation of phosphopeptides derived from bovine casein and dephosphorylation of casein phosphopeptides

โœ Scribed by Goepfert, A. ;Meisel, H.


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
420 KB
Volume
40
Category
Article
ISSN
0027-769X

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โœฆ Synopsis


exchange chromatography. Dephosphorylation of CPP was achieved using immobilized alkaline phosphatase. The purified phosphopeptides and their dephosphorylated forms obtained by these methods are suitable for comparative studies on biological activities, especially mineral binding and immunmodulation.

Semi-preparative isolation of casein phosphopeptides (CPP) from a tryptic hydrolysate of bovine casein was performed applying a three-step procedure consisting of solid phase extraction, reversed phase HPLC and ion


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Studies on in vitro proteolysis of casein using dissolved trypsin or covalently bound to oxirane beads have shown that immobilization leads to a change in the peptide pattern of the resulting proteolysate. Experiments on the variation of the enzyme-substrate ratio (E/S = 1/50, I/lOO, 1/200, 1/400, 1