Abstract
The spatial relationships of major structural proteins within bovine leukemia virus (BLV) particles were investigated by crosslinking with the cleavable bifunctional reagent dimethyl dithiobispropionimidate (DTBPI) or methyl mercaptobutyrimidate (MBI). Covalently linked complexes of viral proteins were analyzed by two-dimensional diagonal polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Both cross-linking reagents produced dimers of p10, p12, p15, and p24 as well as higher oligomers of p10 and p12. Furthermore three heterodimers, p10–p15, p10–p24, and gp30–gp64, were obtained. Surprisingly, BLV isolated in the absence of reducing agents already contained most of these complexes without use of any crosslinking reagents. This result demonstrates close proximities between sulfhydryl groups of certain structural proteins within BLV particles.
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