Four proteins, which have been designated A, B, C and D, have been purified from human parotid saliva. These proteins are the major constituents of parotid saliva which migrate rapidly to the anode in polyacrylamide electrophoresis at pH9.5. Gel filtration and polyacrylamide electrophoresis were employed in the purification procedures. After purification all four preparations were tested for homogeneity by electrophoresis at pH2.8 and 9.5, by isoelectric focusing in the pH range 3–10, by immunodiffusion, and by sedimentation in the analytical ultracentrifuge. None of the proteins showed significant activity in assays for amylase, acid and alkaline phosphatase, protease, lysozyme, ribonuclease, peroxidase, β-glucuronidase, β-galactosidase, iron-binding activity and esterase. No cross-reactions were detected with antisera specific for lactoferrin and 15 serum proteins. All four proteins were rich in glutamic acid, proline and glycine and were lacking completely the sulphur-containing amino acids. Proteins A and C contained no threonine or tyrosine. Carbohydrate could be demonstrated only in protein A at a concentration of 4% of the total protein.
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July 1971
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Research Article|
July 01 1971
Purification and partial characterization of four proteins from human parotid saliva
Anders Bennick;
Anders Bennick
1Department of Biochemistry, University of Toronto, Toronto 5, Ont., Canada
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George E. Connell
George E. Connell
1Department of Biochemistry, University of Toronto, Toronto 5, Ont., Canada
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Publisher: Portland Press Ltd
© 1971 The Biochemical Society
1971
Biochem J (1971) 123 (3): 455–464.
Citation
Anders Bennick, George E. Connell; Purification and partial characterization of four proteins from human parotid saliva. Biochem J 1 July 1971; 123 (3): 455–464. doi: https://doi.org/10.1042/bj1230455
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