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Agar gel electrophoretic demonstration of charge alteration in mutant bacterial proteins
Authors:C R Roe  K S You  N O Kaplan
Affiliation:1. School of Life Science and Technology, Changchun University of Science and Technology, Changchun 130022, PR China;2. School of Science, Changchun University of Science and Technology, Changchun 130022, PR China
Abstract:A mutant of Pseudomonas testosteroni (designated as STDH-m) isolated by Teller and Bongiovanni (1963) is characterized by a highly specific 3-β-AB trans-hydroxysteroid dehydrogenase. Agar gel electrophoretic comparisons of the hydroxysteroid dehydrogenases revealed an anodal change in charge in the mutant enzyme. Numerous other enzymes of the mutant when compared with wild type Ps.testosteroni enzymes were found to be similarly altered in charge. It was also found that all mutant proteins are anodal while the parent organism and a revertant (designated as M3) from the mutant have both anodal and cathodal proteins. These protein alterations are associated with a marked alteration in the buoyant density of the mutant DNA.
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