On the electrophoresis of amylase in gels containing starch

• Published in: Analytical biochemistry Vol. 34; no. 1; pp. 1 - 8
• Main Authors: Boettcher, B., de la Lande, Frances A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.1970
• Subjects: Acrylates; Amylases - analysis; Amylases - blood; Animals; Buffers; Cattle; Drug Stability; Electrophoresis - standards; Gels; Genetics; Humans; Hydrogen-Ion Concentration; Methods; Saliva - enzymology; Starch; Time Factors
• ISSN: 0003-2697; 1096-0309
• DOI: 10.1016/0003-2697(70)90079-5

Electrophoresis of saliva has been performed in polyacrylamide-starch gel slabs in the pH range 4.2 to 10.7. Such gels permit digestion of starch to occur without collapse of the gel matrix. At pH 10.7 starch hydrolysis during electrophoresis is undetectable but, at the other pH's, some starch digestion appears to occur during electrophoresis. At each pH used, amylase appears to interact with starch in the gel. After the completion of electrophoresis, amylase is found throughout a block of gel extending from the sample application slot to the amylase front. The rate of migration of the amylase front is correlated with the amylase concentration in the sample. Observations recorded here, and by other workers, indicate that, irrespective of the source of amylase, interaction occurs between enzyme and gel matrix when amylase is subjected to electrophoresis in a medium containing starch. Consequently, it is concluded that it is inappropriate to subject amylase to electrophoresis in media containing starch, when looking for electrophoretic variants, and that results obtained from electrophoresis under such conditions should be viewed critically.