Purification of the Protein Employed in an Immunodiffusion Test to Diagnose Infectious Bovine Rhinotracheitis

D. J. Brister Department of Veterinary Science and Department of Microbiology, Agricultural Experiment Station, Louisiana State University, Baton Rouge, LA, 70803

L. T. Hart Department of Veterinary Science and Department of Microbiology, Agricultural Experiment Station, Louisiana State University, Baton Rouge, LA, 70803

A. D. Larson Department of Veterinary Science and Department of Microbiology, Agricultural Experiment Station, Louisiana State University, Baton Rouge, LA, 70803

H. D. Braymer Department of Veterinary Science and Department of Microbiology, Agricultural Experiment Station, Louisiana State University, Baton Rouge, LA, 70803

Abstract

The antigen used in an immunodiffusion test to diagnose infectious bovine rhinotracheitis has been purified by affinity chromotography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S˚_20,w of 0.749 was determined and a molecular weight of 8900 was calculated from sedimentation equilibrium analysis. The purified antigen formed precipitin lines of identity with crude diagnostic antigen. Purified antigen remained serologically active in the immunodiffusion test after lyophilization and subsequent reconstitution.

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Purification of the Protein Employed in an Immunodiffusion Test to Diagnose Infectious Bovine Rhinotracheitis

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Purification of the Protein Employed in an Immunodiffusion Test to Diagnose Infectious Bovine Rhinotracheitis

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