Abstract
Atropinesterase and cocainesterase from commercially available, pooled rabbit serum have been resolved using conventional methods of enzyme purification. Using a sequence of ammonium sulfate fractionation, Sephadex G-75 gel filtration and QAE-Sephadex ion exchange chromatography, atropinesterase was purified 750-fold and cocainesterase was purified 220-fold. The two enzymes have been characterized with respect to pH optima. Michaelis constants and substrate specificities. Both hyoscyamine and scopolamine appear to function as substrates for atropinesterase; pH optima and K m determinations arc reported for both substrates. Both cocaine and tropacocaine appear to function as substrates for cocainesterase: pH optima and K m determinations are reported for both substrates with this enzyme.
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