Abstract
Aggregates of barley stripe mosaic virus protein (BSMVp) beginning at the level of 10 S aggregate (i.e., 10 S, 20 S, 30 S, 40 S, etc.) are antigenically identical to each other and to BSMV. The monomeric BSMVp unit is serologically related to, but not identical with, the intact BSMV. The influence of quaternary structure of BSMVp on the conformation of polypeptide chain is discussed. The multiple line formation, with antibody in excess, by the mixtures of antigenically identical BSMVp and BSMV was demonstrated in double-diffusion tests.
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