Document Type
Article
Publication Date
1-1-1992
Abstract
Fresh samples of human whole saliva containing approximately 20-40 micrograms protein were analyzed using SDS-polyacrylamide slab gel electrophoresis systems. More than 20 protein bands were revealed by Coomassie Brilliant Blue R 250 staining. Some of the protein bands were shown to be glycoprotein-positive with PAS (periodic acid-Schiff) reagent. The protein bands with alpha-Amylase activity appeared within a molecular weight range of 120,000-180,000, which is 2 to 2.8 times higher than the normal molecular weight reported for alpha-Amylase from parotid saliva, and showed positive staining with PAS reagent. These results show that the alpha-Amylase in whole saliva appears to exist in a macromolecular form which is not dissociated in the presence of sodium dodecyl sulfate (SDS).
Keywords
Amylase dodecyl sulfate sodium glycoprotein saliva protein article enzymology human molecular weight polyacrylamide gel electrophoresis saliva staining alpha-Amylase Electrophoresis, Polyacrylamide Gel Glycoproteins Salivary Proteins Sodium Dodecyl Sulfate Staining and Labeling Support, Non-U.S. Gov't
Divisions
OralBiology
Publication Title
The Journal of Nihon University School of Dentistry
Volume
34
Issue
4
Additional Information
Cited By (since 1996): 1 Export Date: 10 September 2012 Source: Scopus PubMed ID: 1283755 Language of Original Document: English Correspondence Address: Rahim, Z.H. Chemicals/CAS: amylase, 9000-90-2, 9000-92-4, 9001-19-8; dodecyl sulfate sodium, 151-21-3; alpha-Amylase, EC 3.2.1.1; Glycoproteins; Salivary Proteins; Sodium Dodecyl Sulfate, 151-21-3