Amino Terminal Sequence and Location of Phosphate Groups of the Major Human Casein

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Abstract
The amino acid sequence of the 1st 28 residues of the major human casein was determined. This protein in multiphosphorylated forms (0-5 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 3 of the other phosphorylated forms by examining the aqueous layer of the phenylthiohydantoin conversion step during automatic liquid phase sequencing. Phosphate groups on specific seryl/threonyl residues suggest a biosynthetic mechanism involving stepwise phosphorylation or dephosphorylation.

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