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pubmed:abstractText |
The isolation of a highly purified phosphoprotein, previously named protein A, from human parotid saliva is described. This protein has an unusually high amount of glycine, proline and dicarboxylic amino acids. Together these amino acids account for 80% of all residues. The protein contains 1.9mol of P/mol of protein, probably as phosphate in an ester linkage to serine, and about 0.5% carbohydrate, but no hexosamine. The N-terminal is blocked and the following C-terminal sequence is proposed: -Aal-Asp-Ser-Gln-Gly-Arg-Arg. The sioelectric point is 4.43. The molecular weight of the protein determined by ultracentrifugation is 9900 and from chemical analyses 11000. Circular-dichrosim and nuclea-magnetic-resonance spectra indicate the absence of polyproline and triple-helical-collagen-like structure for the protein. There is little restriction on the orientation of the single phenylalanine residue in the protein., but there is also an indication of conformational restraint in the protein.
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