Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of human parotid salivary proteins. |
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Authors: | J A Beeley D Sweeney J C Lindsay M L Buchanan L Sarna K S Khoo |
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Affiliation: | Dental School Oral Biochemistry Unit (Oral Biology Group), University of Glasgow, UK. |
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Abstract: | The proteins in human parotid saliva have been separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis into 20 or more well resolved species. The Coomassie Brilliant Blue (CBB) R-250 and silver staining procedures have been modified to overcome the problems encountered with staining of proline-rich proteins. By means of the CBB R-250 procedure which stains proline-rich proteins pink-violet, immunoblotting, concanavalin A binding, periodate-Schiff staining and zinc binding, all of the major proteins have been characterised. Substantial individual-to-individual differences were observed in the protein patterns formed. Comparison of parotid, submandibular, and whole saliva from a single individual indicated that fewer proline-rich proteins are expressed in submandibular saliva than in parotid, but whole saliva contains much lower levels than either duct secretion. The results will form a useful base for future research into the functions of salivary proteins. |
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