Examination of Brevibacterium linens by an Electrophoretic Zymogram Technique

SUMMARY: Fifteen isolates of Brevibacterium linens were tested by polyacrylamide gel electrophoresis. Protein patterns and zymograms of 18 intracellular enzyme activities (α-naphthyl acetate and β-naphthyl butyrate esterases, tributyrinase, alcohol-, lactate-, malate-, succinate-, glucose-6-phosphate-, 6-phosphogluconate-, isocitrate-, alanine- and glutamate-dehydrogenases, tetrazolium oxidase, catalase, peroxidase, arylamidase, proteinase and amylase) and four extracellular enzyme activities (α-naphthyl acetate esterase, arylamidase, proteinase and amylase) were examined. Enzyme activities were demonstrated by either specific staining reactions or by the subsequent diffusion of the proteins into a substrate layer. Striking variations of the enzyme patterns occurred among the strains. The variation, however, depended largely on the activity under consideration. Eight different enzymes were selected to calculate a matrix of similarity. The results indicated a separation of the strains into two major subdivisions or biotypes. Only one strain (bl107) differed markedly from the others.