PURIFICATION AND CHARACTERIZATION OF ALEUTIAN DISEASE VIRUS
- 1 September 1980
- journal article
- research article
- Published by Wiley in Acta Pathologica Microbiologica Scandinavica Section B Microbiology
- Vol. 88B (1-6) , 323-328
- https://doi.org/10.1111/j.1699-0463.1980.tb02650.x
Abstract
Virus was isolated from infected mink organs by a combination of tissue homogenization, fluorocarbon extraction and ultracentrifugation. The final preparation was analysed by crossed immunoelectrophoresis and electronmicroscopy. Virions had a capsid diameter of 22 nm. Preparative agarose electrophoresis separated virions from contaminating ferritin. Crossed immunoelectrophoresis of virus gave a single precipitate with sera from infected mink. Crossed immunoelectrophoretic analysis with intermediate gels showed that a part of the virus preparation was complexed with antibody. Serum from a certain mink was found to contain precipitating antibody to (poly)nucleotid. Virus and virus-antibody complexes were found to focus at pH 4.0–4.4 in isoelectric focusing. In SDS-polyacrylamide gel-electrophoresis the main virus protein was found to have a molecular weight of 69000. This study gives further support to the classification of aleutian disease virus as a parvovirus.Keywords
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