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
โฆ LIBER โฆ
Semi-preparative isolation of phosphopeptides derived from bovine casein and dephosphorylation of casein phosphopeptides
โ 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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โฆ 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
๐ SIMILAR VOLUMES
Controlled in vitro proteolysis of casei
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Lorenzen, P. Chr. ;Fischer, H. ;Schlimme, E.
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Article
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1994
๐
John Wiley and Sons
๐
English
โ 408 KB