Abstract |
Using purified equine infectious anemia (EIA) virus labeled with 3H-glucosamine or 14C-protein hydrolysate, structural proteins were analyzed by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. As a result, 2 glycoproteins and 10 proteins with molecular weights (mol wt) ranging from 12,000 to 115,000 daltons were demonstrated. Of 12 structural proteins, 3 proteins, namely a glycoprotein with mol wt of 76,000 (gp76) and 2 proteins with mol wt of 25,000 (p25) and 12,000 (p12), respectively, had distinct antigenic activity from one another in immunodiffusion. Development of antibodies against gp76 and p25 was compared in infected horses. The antibody to gp76 appeared earlier and stronger than to p25 in horses infected with the homologous virus strain. The fraction with glycoproteins was found to have hemagglutinating activity which was inhibited by the serum sample from horses infected with equine infectious anemia virus.
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Authors | M Nishimura, H Nakajima |
Journal | American journal of veterinary research
(Am J Vet Res)
Vol. 45
Issue 1
Pg. 5-10
(Jan 1984)
ISSN: 0002-9645 [Print] United States |
PMID | 6322625
(Publication Type: Comparative Study, Journal Article)
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Chemical References |
- Antibodies, Viral
- Antigens, Viral
- Glycoproteins
- Viral Proteins
- Sodium Dodecyl Sulfate
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Topics |
- Animals
- Antibodies, Viral
(analysis)
- Antigens, Viral
(immunology)
- Centrifugation, Density Gradient
- Electrophoresis, Polyacrylamide Gel
- Equine Infectious Anemia
(immunology)
- Glycoproteins
(immunology)
- Horses
- Immunodiffusion
(veterinary)
- Infectious Anemia Virus, Equine
(analysis, immunology)
- Molecular Weight
- Sodium Dodecyl Sulfate
- Viral Proteins
(immunology)
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