[Characterization of Escherichia hermannii by electrophoresis of esterases, acid phosphatase and glutamate and malate dehydrogenases].

Esterases, acid phosphatase and glutamate and malate dehydrogenases of 11 strains of Escherichia hermannii were analysed by horizontal electrophoresis in polyacrylamide agarose gel. Seven esterase bands were defined by their range of activity on synthetic substrates and their sensitivity or resistance to di-isopropyl fluorophosphate. These bands were different in activity and in mobility from those produced by E. coli strains. On the basis of variations in mobility of glutamate and malate dehydrogenases and in the number and mobility of esterases, the strains were divided into 3 zymotypes.