Histochemical and Pharmacological Evidence of the Function of Butyrylcholinesterase

  • G. B. Koelle
  • W. A. Koelle
  • E. G. Smyrl
  • R. Davis
  • A. F. Nagle
Part of the Advances in Behavioral Biology book series (ABBI, volume 24)


Nearly 40 years ago Alles and Hawes (1) demonstrated that the cholines-terases (ChE) of erythrocytes and plasma differ. The work of Mendel and associates (26, 27), Nachmansohn (29), Augustinsson (2, 3) and others clearly established the distinguishing characteristics between acetylcholinesterase (also called specific, or true ChE, ACh hydrolase; EC3.1.1.7; A ChE) and butyrylcholinesterase (non-specific or pseudo-ChE, acylcholine acyl-hydrolase; EC 3.1.1. 8; BuChE). The former enzyme predominates in the central nervous system (CNS), the motor endplates (MEPs) of skeletal muscle, and erythrocytes, and the latter in many types of smooth muscle, the liver and plasma; both enzymes occur in high concentrations in autonomic ganglia (16). The substrate concentration-velocity of hydrolysis curves for ACh and other Ch esters with A ChE are bellshaped, with the peaks at approximately 0. 003 M. ACh is hydrolyzed most rapidly, methacholine (MeCh) at about one-third and butyrylcholine (BuCh)at only a small percent of the rate of ACh, and benzoylcholine (BzCh) insignificantly. BuChE shows typical sigmoid, Michaelis-Menten type substrate-velocity curves, with the highest rate for BuCh, followed by ACh and BzCh, and practically no hydrolysis of MeCh.


AChE Activity Superior Cervical Ganglion Motor Endplate Autonomic Ganglion Ciliary Ganglion 
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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • G. B. Koelle
    • 1
  • W. A. Koelle
    • 1
  • E. G. Smyrl
    • 1
  • R. Davis
    • 1
  • A. F. Nagle
    • 1
  1. 1.Department of PharmacologyUniversity of Pennsylvania Medical SchoolPhiladelphiaUSA

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