Protein from particles of rice gall dwarf virus was resolved into seven components by polyacrylamide gel electrophoresis. The estimated molecular weights (× 10) were 183, 165, 150, 143, 120, 56 and 45 (K). Cores prepared by treating intact particles with CsCl contained the 183K, 165K, 120K and 56K proteins; the 150K, 143K and 45K proteins were recovered from the top layer of gradients after CsCl equilibrium centrifugation. Antiserum against intact particles reacted mainly with 150K and 45K proteins and antiserum against core particles reacted mainly with 183K and 120K proteins. The results suggest that the 150K and 45K proteins are located on the surface of the outer capsid, that the 183K and 120K proteins are on the surface of the core, that the 165K and 56K proteins are inside the core, and that the 143K protein is either inside the outer capsid or inside the core.

Keyword(s): core , immunoblotting , protein and RGDV

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