PMID: 701270Oct 25, 1978Paper

Fractionation of human parotid saliva proteins.

The Journal of Biological Chemistry
R I HenkinH Edelhoch

Abstract

A chromatographic procedure for purification of the proteins in human parotid saliva has been developed. The eluates of a Sephadex G-150 and two ion exchange columns have been analyzed simultaneously by several physical and chemical tests; these include three optical properties of proteins, assays for neutral sugars, sialic acid and zinc, and disc gel electrophoresis. The ratios of the different variables have been used to determine the homogeneity and complexity of the protein distribution in the various peaks of the chromatographic eluates. By chromatographic methods, it has been possible to purify a glycoprotein with unusual staining characteristics and amino acid composition. Glycoproteins with similar properties comprise a major portion of the proteins in parotid saliva and appear to constitute a family of related proteins which differ in molecular size, carbohydrate and sialic acid content, and electrophoretic mobility. The fractionation of several enzymes in parotid saliva is also reported.

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The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

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