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PURIFICATION AND PROPERTIES OF BRAIN ACETYL-CHOLINESTERASE (EC 3.1.1.7)1

Authors

  • S. L. Chan,

    1. Department of Pharmacology, University of California Medical Center, San Francisco, California 94122
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    • 2

      Recipient of a U.S.P.H.S. post-doctoral fellowship (277-MH7082).

  • D. Y. Shirachi,

    1. Department of Pharmacology, University of California Medical Center, San Francisco, California 94122
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    • 3

      Recipient of a U.S.P.H.S. post-doctoral fellowship (US-39008).

  • A. J. Trevor

    1. Department of Pharmacology, University of California Medical Center, San Francisco, California 94122
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  • 1

    This work was supported by a grant from the National Institutes of Health GM-(13835).

Abstract

Abstract— Approximately 50 per cent of the total AChE of brain tissue was solubilized by a simple procedure of repeated homogenization and centrifugation in 0.32 M-sucrose containing EDTA. Ion-exchange and molecular-sieve chromatography demonstrated two peaks of AChE activity which apparently differed with respect to charge properties and molecular size. The most active preparation of AChE, which hydrolysed 13,500 μMmoles of acetylthiocholine/mg of protein/h, had an estimated molecular weight of 291,000 and was contaminated by a single protein component, as judged by disc gel electrophoresis.

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