Detection of beta-1,3-glucanase activity after native polyacrylamide gel electrophoresis: application to tobacco pathogenesis-related proteins

Electrophoresis
F CôtéA Asselin

Abstract

Beta-1,3-Glucanase (laminarinase) activity was detected after polyacrylamide gel electrophoresis under native conditions by using laminarin as substrate. Following incubation of gels, laminarin was stained with Aniline Blue. Under UV illumination, lysis zones appeared as dark bands against a fluorescent background. As low as 0.001 unit of commercial Penicillium laminarinase could be observed after incubating the polyacrylamide gel for 45 min at pH 5.0. Extracts of commercial Penicillium laminarinase exhibited four bands with lytic activity towards laminarin. Analysis of intercellular fluid extracts of tobacco mosaic virus-infected tobacco leaves revealed four beta-1,3-glucanases corresponding to three acidic pathogenesis-related proteins, b4 (2), b5 (N) and b6b (0), and one basic protein. The presence of laminarin in gels retarded the migration of some proteins with beta 1,3-glucanase activity. This change in electrophoretic mobility could be used as a complementary affinity test for identifying proteins with beta-1,3-glucanase activity.

References

Dec 1, 1973·Analytical Biochemistry·K E Eriksson, B Pettersson
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

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Citations

Dec 10, 1998·Plant Physiology·J TrudelA Asselin
Jun 1, 1992·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·G W SchaefferJ T Dudley

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