Marek's Disease Herpesviruses II. Purification and Further Characterization of Marek's Disease Herpesvirus A Antigen 1

作者: Philip A. Long , James L. Clark , Leland F. Velicer

DOI: 10.1128/JVI.15.5.1192-1201.1975

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摘要: Abstract Marek's disease herpesvirus A antigen was purified greater than 200-fold with a 24% recovery by ion exchange column chromatography, isoelectric focusing, and preparative polyacrylamide gel electrophoresis. The had an point of 6.68 ± 0.03 in the presence 1 M urea 0.05% Brij 35, nonionic detergent, approximately 6.5 absence dissociating agents. When analyzed electrophoresis on analytical gels, migrated as single broad band which stained for both protein carbohydrate, suggesting that it highly heterogeneous glycoprotein. However, not to homogeneity determined gels sodium dodecyl sulfate immunodiffusion analysis. Antibody Marek's prepared rabbit, antibody two contaminating antigens removed adsorption yield monospecific antisera.

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