Selective dansylation of M protein within intact influenza virions
Exposure of purified influenza virions to (/sup 14/C)dansyl chloride resulted in the covalent attachment of the dansyl chromophore to the virion. Gel electrophoresis revealed that the dansyl chromophore was specifically coupled to the internal membrane (M) protein. Purification of the M protein by gel filtration followed by cyanogen bromide cleavage and peptide fractionation revealed that four of six peptide peaks contained dansyl label. Acid hydrolysis of the separated peptide peaks followed by thin-layer chromatography revealed that dansyl label was coupled to lysine residues present in these peptides. The results of these investigations have demonstrated that the M protein molecule is the major viral polypeptide labeled when intact virions are exposed to dansyl chloride.
- Research Organization:
- Department of Microbiology, University of Alabama, Birmingham
- OSTI ID:
- 6149455
- Journal Information:
- J. Virol.; (United States), Vol. 44:3
- Country of Publication:
- United States
- Language:
- English
Similar Records
Association of Sendai virion envelope and a mouse surface membrane polypeptide on newly infected cells: lack of association with H-2K/D or alteration of viral immunogenicity
Purification of the labeled cyanogen bromide peptides of the. cap alpha. polypeptide from sodium and potassium ion-activated adenosinetriphosphatase modified with N-(/sup 3/H)ethylmaleimide
Related Subjects
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
CARBON 14 COMPOUNDS
CHEMICAL PREPARATION
ELECTROPHORESIS
INFLUENZA VIRUSES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
THIN-LAYER CHROMATOGRAPHY
USA
CHROMATOGRAPHY
MICROORGANISMS
NORTH AMERICA
ORGANIC COMPOUNDS
PARASITES
SEPARATION PROCESSES
SYNTHESIS
VIRUSES
550201* - Biochemistry- Tracer Techniques