Abstract
It was shown by gel chromatography, sucrose gradient centrifugation and immunodiffusion that tobacco rattle virus (TRV) coat protein can exist in various discrete states of aggregation. Mol. wt. values of about 20000, 75000 and 210000 were estimated for the coat protein subunit and two discrete oligomeric aggregates, and a sedimentation coefficient of about 35S for the characteristic disc-like polymeric aggregate. Some serological differences between the 35S-aggregate and a mixture of oligomers and monomers of the coat protein subunit were demonstrated by agar gel immunodiffusion and immunoelectrophoresis.
* Present address: Division of Virology, Department of Pathology, University of Cambridge, Cambridge, U.K.