Abstract
Lactate dehydrogenase and alkaline phosphatase isoenzymes of the Mongolian gerbil were examined using electrophoretic techniques and were compared with those of the mouse, rat, and guinea pig. Five isoenzymes of lactate dehydrogenase (LDH) were detected in the gerbil with LDH2 and LDH5 being equally dominant. Two bands of alkaline phosphatase (ALP) were distinguished in sera treated with neuraminidase in the gerbil and the relative activity of the cathodic fraction was greater than those of the mouse and rat. Genetic polymorphism was not found among the coat color variants of the Mongolian gerbil. A comparative study on LDH and ALP revealed distinct interspecific differences in the rate of the electrophoretic migration of the respective isoenzymes among the mouse, rat, guinea pig, and the Mongolian gerbil.
