Electrophoretic detection of salivary alpha-amylase activity

Rahim, Z.H. and Yaacob, H.B. (1992) Electrophoretic detection of salivary alpha-amylase activity. The Journal of Nihon University School of Dentistry, 34 (4). pp. 273-277. ISSN 0029-0432,


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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).

Item Type: Article
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; Glycoproteins; Salivary Proteins; Sodium Dodecyl Sulfate, 151-21-3
Uncontrolled 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
Subjects: R Medicine > RK Dentistry
Divisions: Faculty of Dentistry > Dept of Oral Biology
Depositing User: Mr Ahmad Azwan Azman
Date Deposited: 10 Oct 2012 01:52
Last Modified: 10 Oct 2012 01:52
URI: http://eprints.um.edu.my/id/eprint/3750

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