Lactic dehydrogenase brain tissue

Pb(C2H5)4 reduces lactic dehydrogenase activity in rabbit tissues, but has no effect on aminopeptidase and acid phosphatase. The anti-monoamine oxidase activity of Pb(C2H5)4 is thought to be due to other metabolic disturbances [221]. No differences were found in the oxygen consumption and phosphorylation in brain, lung, and liver tissues of rabbits poisoned by Pb(C2H5)4 [126]. 

Lactic dehydrogenase, accompanied by its co-enzyme, is present in muscle, brain and other tissues, and in yeast. It dehydrogenates lactic into pyruvic acid. 

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