Purification and characterization of Aleutian disease virus.
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.
D000454:Aleutian Mink Disease Virus / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D000936:Antigen-Antibody Complex / Q000032:analysis; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007123:Immunoelectrophoresis, Two-Dimensional; D007525:Isoelectric Focusing; D008907:Mink / Q000382:microbiology; D008970:Molecular Weight; D009711:Nucleotides / Q000032:analysis; D010455:Peptides / Q000032:analysis; D014713:Viruses, Unclassified / Q000302:isolation & purification*
D000936:Antigen-Antibody Complex; D009711:Nucleotides; D010455:Peptides