Polyacrylamide gel electrophoresis and isoelectric focusing techniques have
been used to compare NAD-dependent L( + )lactate dehydrogenases (LDH) fromten different strains of Mycoplasma mycoides var. mycoides. The enzymes were not distinguished from one another, or from normal bovine LDH I by these methods. The kinetic behaviour of LDH from M. mycoides (Tl vaccine strain) suggested that the enzyme could readily reduce pyruvate or oxidize lactate in a manner which, in vertebrates, requires two different isoenzymes.
