Electrophoretic detection of salivary alpha-amylase activity.
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).
Rahim
Z H
ZH
Dental Faculty, University of Malaya, Kuala Lumpur, Malaysia.
Yaacob
H B
HB
D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis; D006801:Humans; D008970:Molecular Weight; D012463:Saliva / Q000201:enzymology*; D012471:Salivary Proteins and Peptides / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate; D013194:Staining and Labeling; D000516:alpha-Amylases / Q000032:analysis*
D006023:Glycoproteins; D012471:Salivary Proteins and Peptides; D012967:Sodium Dodecyl Sulfate; D000516:alpha-Amylases