Abstract
Cowpea mosaic virus protein was resolved into two polypeptide size classes by polyacrylamide gel electrophoresis in urea plus sodium dodecyl sulfate and by gel permeation chromatography in urea solution. Molecular weights of 22,000 and 42,000 were estimated for these size classes. Amino acid and peptide analyses indicated that each class consisted of a single kind of polypeptide chain. Evidence was obtained for the existence of some amino acid sequences common to the two proteins, but the possibility of a monomer-dimer relationship was excluded. Approximately equimolar amounts of the two proteins were found in each of the three centrifugal components of the virus: top, middle, and bottom.
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