Inactivation of the Catalytic Activities in Human Serum Butyrylcholinesterase by Metal Chelators

  • C. D. Bhanumathy
  • A. S. Balasubramanian

Abstract

Human serum butyrylcholinesterase (BChE) which shows 53% of sequence identity to acetylcholinesterase (AChE) exhibits an arylacylamidase (AAA) and a peptidase activity. Earlier studies in our laboratory have shown that the peptidase activity in BChE was inhibited by metal chelators and metal ions can stimulate the peptidase activity. (Rao and Balasubramanian, 1993). In pursuance of those studies we describe now that metal chelators can inhibit not only the peptidase but also the cholinesterase and AAA activities.

Keywords

Zinc EDTA Lipase Histidine Diamine 

References

  1. Cygler, M., Schrag, J.D., Sussman, J.L., Harel, M., Silman, I., Gentry, M.K., and Doctor, B.P., 1993, Relationship between sequence conservation and three-dimensional structure in a large family of esterases, Upases and related proteins, Protein Science 2, 366–382.PubMedCrossRefGoogle Scholar
  2. Rao, R.V., and Balasubramanian, A.S., 1993, The peptidase activity of human serum butyrylcholinesterase: Studies using monoclonal antibodies and characterization of the peptidase, J. Protein. Chem. 12, 103–110.PubMedCrossRefGoogle Scholar
  3. Balasubramanian, A.S., and Bhanumathy, C.D., 1993, Noncholinergic functions of cholinesterases, FASEB J. 7, 1354–1358.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • C. D. Bhanumathy
    • 1
  • A. S. Balasubramanian
    • 1
  1. 1.Neurochemistry LaboratoryChristian Medical College and HospitalVelloreIndia

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