Electrophoretic protein patterns and enzyme mobilities in anaerobic coryneforms.
The soluble protein patterns and electrophoretic mobilities of malate and succinate dehydrogenases and catalase have been examined in 25 strains of Propionibacterium acnes, P. granulosum, and P. avidum. A distinctive protein pattern for each species was found, and it was possible also to distinguish the serotypes within P. acnes and P. avidum. Strains of P. acnes, P. granulosum, and P. avidum could be differentiated by the mobilities of their malate dehydrogenases. Catalase activity was detected in the soluble fractions of all strains. Catalases from P. acnes and P. avidum strains had the same mobility, whereas that from P. granulosum was slightly slower. Under the conditions used, succinate dehydrogenase activity could be detected, but the patterns were not distinctive.
D000693:Anaerobiosis; D001426:Bacterial Proteins / Q000032:analysis*; D002374:Catalase / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008291:Malate Dehydrogenase / Q000378:metabolism*; D011424:Propionibacterium / Q000032:analysis* / Q000201:enzymology; D011425:Propionibacterium acnes / Q000032:analysis* / Q000201:enzymology; D012995:Solubility; D013045:Species Specificity; D013385:Succinate Dehydrogenase / Q000378:metabolism*
D001426:Bacterial Proteins; D008291:Malate Dehydrogenase; D002374:Catalase; D013385:Succinate Dehydrogenase