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Members of a family of acidic proteins taken from human submandibular-sublingual saliva were designated cysteine-containing phosphoproteins, since they could be distinguished from other salivary phosphoproteins by the presence of half-cystine. These molecules consisted of a single peptide chain of approximately 14,000 daltons. Their isoelectric points ranged from 4.3 to 5.9. Two groups (C2 and C3) were O-phosphorylated. Their charge heterogeneity was apparently due to variations in content of phosphate and acidic and basic amino acids.
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