Abstract
The coat protein from purified particles of pea seedborne mosaic potyvirus (PSbMV) moves in SDS-PAGE with an apparent molecular weight ( M r) of 36 kDa. However, extracts of PSbMV infected plants prepared with SDS or urea contain PSbMV immunoreactive proteins with apparent ( M r) 39 kDa as well as 36 kDa. The low mobility form may be generated from the apparent ( M r) 36 kDa form by incubating purified PSbMV particles with healthy plant sap in the presence of denaturing agents. A similar effect is observed with bean yellow mosaic potyvirus, but not with three viruses outside the potyvirus group. Experiments suggest that a soluble plant enzyme is responsible for the conversion, which apparently takes place only in vitro under denaturing conditions. This phenomenon may lead to erroneous conclusions about the ( M r) of some viral coat proteins. However, the conversion can be prevented by heat treatment of the plant tissue prior to extraction.
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