U.S. flag An official website of the United States government.
Official websites use .gov

A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS

A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

i

Characterization of [3H]di-Isopropyl Phosphorofluoridate-Binding Proteins in Hen Brain. Rates of Phosphorylation and Sensitivity to Neurotoxic and Non-Neurotoxic Organophosphorus Compounds



Details

  • Personal Author:
  • Description:
    The experiments described in this paper were designed to isolate [3H]di-isopropyl phosphorofluoridate-binding proteins by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis for the purpose of characterizing and identifying potential initiation sites for organophosphorus-compound-induced delayed neurotoxicity. The major Paraoxon-insensitive Mipafox-sensitive binding protein (Mr 160 000) was found to be identical with one previously identified as neurotoxic esterase, an enzyme that has been proposed to be the target site for organophosphorus-compound-induced delayed neurotoxicity. However, two other binding proteins with suitable binding characteristics were also found in smaller amounts, one of which has not been detected previously. Di-isopropyl phosphorofluoridate was found to phosphorylate all three of these proteins at rates similar to the rate at which neurotoxic esterase is inhibited by di-isopropyl phosphorofluoridate. Varying the concentration of di-isopropyl phosphorofluoridate or the time of incubation produced similar increases in binding to each of the labelled proteins. This suggests that the reaction rates of di-isopropyl phosphorofluoridate with proteins may be described by first-order kinetics, and the concentration of the Michael is complex formed during binding is minimal for all the phosphorylated proteins. The recovery of the binding activity in the 160 000-Mr band was found to be similar to the recovery of neurotoxic esterase activity, lending further support to the contention that this band is identical with neurotoxic esterase. [Description provided by NIOSH]
  • Subjects:
  • Keywords:
  • ISSN:
    0264-6021
  • Document Type:
    Text
  • Funding:
    Grant
  • Genre:
    Journal Article
  • Place as Subject:
  • CIO:
    National Institute for Occupational Safety and Health (NIOSH)
  • Topic:
    Workplace Safety & Health
  • Location:
    North America
  • Volume:
    228
  • Issue:
    3
  • NIOSHTIC Number:
    nn:20037419
  • Citation:
    Biochemical J 1985 Jun; 228(3):537-544
  • Contact Point Address:
    Mohamed B. Abou-Donia, Department of Pharmacology, Duke University Medical Center, Durham, NC 27710, U.S.A.
  • Federal Fiscal Year:
    1985
  • Performing Organization:
    Duke University, Durham, North Carolina
  • Peer Reviewed:
    True
  • Start Date:
    19840601
  • Source Full Name:
    Biochemical Journal
  • End Date:
    19881031
  • Collection(s):
  • Main Document Checksum:
    urn:sha-512:2fa9d270a5bd8f7d55f14e4c87afce842b7dd43a9acbbf921557f821e3e33d1fc1f0982d207a3ff0494e21d55b4dc53128eb3bb6fa9ceb1ad5085a68612c1816
  • Download URL:
  • File Type:
    Filetype[PDF - 1.33 MB ]
PREVIOUS
ON THIS PAGE
Details
CDC STACKS serves as an archival repository of CDC-published products including scientific findings, journal articles, guidelines, recommendations, or other public health information authored or co-authored by CDC or funded partners.

As a repository, CDC STACKS retains documents in their original published format to ensure public access to scientific information.
BACK TO TOP