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A rapid method for separation and detection of human salivary amylase isoenzymes by isoelectric focusing in polyacrylamide gel
Author(s) -
WADSTRÖM TORKEL,
NORD CARLERIK,
KJELLGREN MARIANNE
Publication year - 1976
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1976.tb00485.x
Subject(s) - isoelectric focusing , chromatography , agarose , amylase , chemistry , saliva , polyacrylamide , polyacrylamide gel electrophoresis , isoelectric point , tris , biochemistry , enzyme , polymer chemistry
– Human salivary proteins were separated by isoelectric focusing on polyacrylamide gel in flat beds at 1000 V for 40 min. Amylase activity was detected after immersing the gel in 0.4 M tris‐HCl buffer pH 7.4 to equilibrate the pH gradient. The enzyme activity was detected after diffusion into an overlayer of agarose gel containing an insoluble dye‐starch polymer (Phadebas®). Both whole human saliva and parotid saliva from 15 different persons contained four amylase components, except in three cases where only three bands were detected. The bands were all focused within a rather narrow pH range (pH 5.4–7.2) and the results were very reproducible.