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Inhibition of Cholinesterase Hydrolysis of Dihydromurexine by Lysergic Acid Diethylamide and its 2-Bromo Derivative: a Selective Relationship

Nature volume 182, page 935 (1958)Cite this article

Abstract

PREVIOUS investigators have shown that human plasma cholinesterase is strongly inhibited by both lysergic acid diethylamide (LSD) and its 2-bromo derivative (BOL). The cholinesterases of other species were less sensitive to the effects of both these substances1–3. Recent reports described certain newer choline esters, namely, imidazoleacrylylcholine4 5 (murexine), imidazoleacetylcholine6 and imidazolepropionylcholine (dihydromurexine) which are hydrolysed most readily by human plasma cholinesterase7–10. These observations have led us to evaluate the possible relationship between cholinesterase inhibition by lysergic acid diethylamide and BOL and cholinesterase hydrolysis of dihydromurexine. Dihydromurexine was chosen as the model substrate because it is the most active of the three esters.

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References

  1. Thompson, R. H. S., Tickner, A., and Webster, G. R., Brit. J. Pharmacol., 10, 61 (1955).

    PubMed  CAS  PubMed Central  Google Scholar 

  2. Zehnder, V. K., and Cerletti, A., Helv. Physiol. Pharmacol. Acta, 14, 264 (1956).

    PubMed  CAS  Google Scholar 

  3. Fried, G. H., and Antopol, W., J. App. Physiol., 11, 25 (1957).

    Article  CAS  Google Scholar 

  4. Erspamer, V., and Benati, O., Science, 117, 161 (1953).

    Article  ADS  CAS  PubMed  Google Scholar 

  5. Keyl, M. J., Michaelson, I. A., and Whittaker, V. P., J. Physiol., 139, 434 (1957).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  6. Grunert, G., and Kewitz, H., Naturwiss., 42, 628 (1955).

    Article  ADS  Google Scholar 

  7. Foldes, F. F., Erdös, E. G., Baart, N., and Shanor, S. P., Proc. Soc. Exp. Biol. N.Y., 94, 500 (1957).

    Article  CAS  Google Scholar 

  8. Grelis, M. E., and Tabachnick, I. I. A., Brit. J. Pharmacol., 12, 320 (1957).

    PubMed  CAS  PubMed Central  Google Scholar 

  9. Keyl, M. J., and Whittaker, V. P., Brit. J. Pharmacol., 13, 103 (1958).

    PubMed  CAS  PubMed Central  Google Scholar 

  10. Tabachnick, I. I. A., Roth, F. E., Mershon, J. S., Rubin, A. A., Eckhardt, E. T., and Govier, W. M., J. Pharmacol., 123, 98 (1958).

    CAS  Google Scholar 

  11. Hestrin, S., J. Biol. Chem., 180, 249 (1949).

    PubMed  CAS  Google Scholar 

Download references

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Authors and Affiliations

  1. Department of Pharmacology, Scientific Research Division, Schering Corporation, Bloomfield, New Jersey

    I. I. A. TABACHNICK & M. E. GRELIS

Authors
  1. I. I. A. TABACHNICK
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  2. M. E. GRELIS
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TABACHNICK, I., GRELIS, M. Inhibition of Cholinesterase Hydrolysis of Dihydromurexine by Lysergic Acid Diethylamide and its 2-Bromo Derivative: a Selective Relationship. Nature 182, 935 (1958). https://doi.org/10.1038/182935a0

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