Jan 1, 1976

Purification, characterization, and quantitation of the antigen employed in the immunodiffusion test for diagnosis of equine infectious anemia

Preparative Biochemistry
L T HartE A Broussard

Abstract

Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4 fractionation 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.

Mentioned in this Paper

Spleen
Erythrocyte Sedimentation Rate Measurement
Antigens
Purification Aspects
Sedimentation Procedure
Chemical Fractionation
Spleen Tissue
Drug Stability
Acids
Equine Infectious Anemia

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