Abstract
The steps from the precursor to the processed forms of a secreted glycoprotein (gA) of Marek's disease virus (MDV) and of herpesvirus of turkeys (HVT) were examined by two-dimensional gel electrophoresis of immunoprecipitates from the cell lysate and medium of infected cultures with monoclonal antibodies. Differences between MDV-and HVT-gA were particularly observed in isoelectric points of the glycosylated or unglycosylated precursor forms.