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Characterization of Cysteine-containing Phosphoproteins from Human Submandibular-Sublingual Saliva

Department of Oral Biology, School of Dentistry, State University of New York at Buffalo, Buffalo, New York 14226

L.A. Tabak

Department of Oral Biology, School of Dentistry, State University of New York at Buffalo, Buffalo, New York 14226

M.J. Levine

Department of Oral Biology, School of Dentistry, State University of New York at Buffalo, Buffalo, New York 14226

I.D. Mandel

School of Dental and Oral Surgery, Columbia University, New York, New York 10032

S.A. Ellison

School of Dental and Oral Surgery, Columbia University, New York, New York 10032

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 ~ 14,000 daltons. Their isoelectric points ranged from 4.3 to 5.9. Two groups (C2 and C3) were 0-phosphorylated. Their charge heterogeneity was apparently due to variations in content of phosphate and acidic and basic amino acids.

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Journal of Dental Research, Vol. 61, No. 6, 764-767 (1982)
DOI: 10.1177/00220345820610062201


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