Abstract
Three disulphide cross-bridged glycoprotein complexes were immunoprecipitated from purified human cytomegalovirus envelopes using a monoclonal antibody with a specificity for a glycoprotein of mol. wt. 52 X 10(3). These complexes were isolated by electroelution after polyacrylamide gel electrophoresis (PAGE) under non-reducing conditions. Compositional analysis of each complex by PAGE under reducing conditions showed that at least two distinct complexes, one containing glycoproteins with mol. wt. of 52 X 10(3) and 95 X 10(3) and the other with glycoproteins of 52 X 10(3) and 130 X 10(3), were present. The results obtained indicated that one of these complexes could also exist as a dimer.