Study of Toxic and Antigenic Structures of Botulinum Neurotoxin

Abstract

Analysis of the secondary structures of the isolated light and heavy chains of type A neurotoxin (NT) by circular dichroism showed that the two subunit chains did not undergo significant structural changes when separated from each other. Nicking of the single chain type E into the dichain form brought about conformational changes that were detected based on ionization of tyrosine residues. Both the light and heavy chains of types A, B, and E NTs were found to attach to the lipid bilayer surface. Parameters of Fast Protein Liquid Chromatography of type A, B, and E NTs were developed.

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Document Details

Document Type
Technical Report
Publication Date
May 26, 1988
Accession Number
ADA202844

Entities

People

  • B. R. Dasgupta

Organizations

  • University of Wisconsin–Madison

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Abstracts
  • Amino Acids
  • Availability
  • Biomedical Research
  • Chemistry
  • Chromatography
  • Classification
  • Dichroism
  • Ion Exchange
  • Ionization
  • Laboratory Animals
  • Lipids
  • Liquid Chromatography
  • Membrane Lipids
  • Molecules
  • Security
  • Spectra

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry