title: Separation of the proteins of rat parotid saliva by hydrophobic-interaction chromatography.
abstract: Parasympathetically-evoked rat parotid salivary proteins were resolved into 11 peaks by hydrophobic-interaction chromatography. SDS-PAGE indicated that most peaks contained a single major component and that only one major protein was not chromatographed. The findings indicate that hydrophobic-interaction chromatography can be used in the quantification of changes in individual salivary proteins under different experimental conditions, and in the purification of individual salivary proteins.
authors: Department of Oral Pathology, King's College School of Medicine and Dentistry, London, England.
authors: G B
authors: GB
authors: Proctor
authors: B
authors: B
authors: Mansson
mesh_terms: D000818:Animals; D002845:Chromatography / Q000379:methods; D003545:Cysteine / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007930:Leucine / Q000302:isolation & purification; D010306:Parotid Gland / Q000737:chemistry*; D010455:Peptides / Q000302:isolation & purification; D055232:Proline-Rich Protein Domains; D051381:Rats; D011919:Rats, Inbred Strains; D012471:Salivary Proteins and Peptides / Q000302:isolation & purification*; D012967:Sodium Dodecyl Sulfate
chemical_list: D010455:Peptides; D012471:Salivary Proteins and Peptides; D012967:Sodium Dodecyl Sulfate; D007930:Leucine; D003545:Cysteine