Purification, Characterization, and Quantitation of the Antigen Employed in the Immunodiffusion Test for Diagnosis of Equine Infectious Anemia
- 31 December 1975
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 6 (2-3), 193-211
- https://doi.org/10.1080/00327487608061612
Abstract
Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4fractionation and affinity chromatography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S20, w of 0.51 was determined and a molecular weight of 7600 was calculated from sedimentation equilibrium analysis. The amino acid composition of the pure antigen indicated the antigen is an acidic protein. Employing radical immunodiffusion (RID) and pure antigen a method for quantitating antigen content of antigen containing preparations was developed.Keywords
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