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Eastern Regional Research Center1, Philadelphia, PA 19118
ABSTRACT
The amino acid sequence of the first 28 residues of the major human casein was determined. This protein in multi-phosphorylated forms (0 to 5 phosphorous per molecule) was compared to cow beta-casein which is similar in composition but phosphorylated at a constant level. After sequencing the phosphate-free human casein, phosphorylated seryl and threonyl residues were located in three of the other phosphorylated forms by examining the aqueous layer of the phenylthio-hydantoin conversion step during automatic liquid phase sequencing. Phosphate groups on specific seryl/threonyl residues suggest a biosynthetic mechanism involving stepwise phosphorylation or dephosphorylation.
1 Agricultural Research Service, US Department of Agriculture.
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