Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of human parotid salivary proteins.
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.
Beeley
J A
JA
Dental School Oral Biochemistry Unit (Oral Biology Group), University of Glasgow, UK.
Sweeney
D
D
Lindsay
J C
JC
Buchanan
M L
ML
Sarna
L
L
Khoo
K S
KS
D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015151:Immunoblotting; D010306:Parotid Gland / Q000378:metabolism*; D011392:Proline / Q000032:analysis; D011485:Protein Binding; D012394:Rosaniline Dyes; D012463:Saliva / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000302:isolation & purification*; D016622:Silver Staining; D015037:Zinc Radioisotopes
D012394:Rosaniline Dyes; D012471:Salivary Proteins and Peptides; D015037:Zinc Radioisotopes; C024757:Coomassie brilliant blue R; D011392:Proline