Cholinesterases in Rat Liver Mitochondria

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Abstract
The selective staining of mitochondria from various sources by Janus Green B and Methylene Blue and the acetylcholine-like activity of these dyes on the clam and frog heart as well as their potent inhibition of horse serum cholinesterase led to the assay of mitochondria for specific and nonspecific cholinesterase. Mitochondria were prepared by differential centrifugation of rat liver homogenate prepared in isotonic sucrose. Homogenate, mitochondria and supernatant fractions were assayed for cholinesterase by the Warburg manometric procedure. Enzyme specificity was determined by measuring hydrolysis of benzoyl choline and acetyl-[beta]-methyl choline. Mitochondria contained more nonspecific than specific cholinesterase. Microsome fractions, separated by prolonged centrifugation of the supernatant obtained in the separation of mitochondria, possessed high cholinesterase activity probably due to mitochondrial fragmentation. The attraction of cholinesterase receptor groups for the alkylated quaternary nitrogen groups of Janus Green B and similar basic dyes may be responsible for the staining of mitochondria from liver and the motor end plate by these dyes.

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