Characterization of glycoprotein complexes present in human cytomegalovirus envelopes.
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.
D000911:Antibodies, Monoclonal / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D003587:Cytomegalovirus / Q000032:analysis* / Q000276:immunology; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D007122:Immunoelectrophoresis; D014759:Viral Envelope Proteins / Q000276:immunology / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D006023:Glycoproteins; D014759:Viral Envelope Proteins