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An antigenic analysis of potato virus X and of its degraded protein

Virology, ISSN: 0042-6822, Vol: 42, Issue: 4, Page: 835-847
1970
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  • Citations
    21
    • Citation Indexes
      21
  • Captures
    1

Article Description

The hydrodynamic properties of pyridine-degraded structural protein (D-protein) of potato virus X (PVX) were investigated. Sephadex chromatography and analytical centrifugation revealed that some preparations of D-protein in aqueous buffers contained primarily homogeneous dimeric structural units. Other preparations contained a mixture of monomers and dimers. Electrophoretic analysis gave a monomeric molecular weight of 25,000. D-protein solutions had properties characteristic of denatured globular proteins in solution, i.e., they eluted from Sephadex G-200 earlier than expected for their particular molecular weights, and they possessed high frictional ratios and intrinsic viscosities. Also, the Stokes radius of the depolymerized monomer was nearly twice that of the structural units in intact nucleocapsids. It was concluded that the structural unit undergoes a major change in conformation on depolymerization and that a concomitant formation of new antigenic determinants most probably accounts for the antigenic disparity between D-protein and PVX.

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