Abstract
Dehydrogenase distributions were determined with Nitro BT in fresh flat mounts of the rabbit lens epithelium and capsule. The capsule was unreactive and the epithelium displayed high lactic and malic dehydrogenase activities, and minimal uridine diphosphate glucose and glucose-6-phosphate dehydrogenase activities. In addition, lactic and malic dehydrogenases were present in higher amounts in the peripheral (pre-equatorial and equatorial) than in the central areas of the epithelium. Lactic dehydrogenase activity was specifically inhibited by sodium and potassium iodide, oxalic acid and sodium pyruvate, the latter effect reversed with cyanide. High lactic dehydrogenase activity in lens epithelium correlates adequately with previous microchemical determinations and points to a possible role of the epithelium in the active lactate production of the lens.