title: [Isolation and purification of 3C-proteinase from the poliomyelitis virus. Identification of an active form of the enzyme].
abstract: All the forms of 3C protease previously found were isolated and purified. A 3D polymerase's fragment covalently bound with 3C protein does not affect the specific proteolytic activity of the enzyme, whereas the elimination of 26 N-terminal amino acid residues of 3C protease leads to its inactivation.
authors.forename: E P
authors.initials: EP
authors.lastname: Sablina
authors.forename: V K
authors.initials: VK
authors.lastname: Antonov
mesh_terms: D002853:Chromatography, Liquid; D003001:Cloning, Molecular; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D005822:Genetic Vectors; D017955:Poliovirus / Q000201:enzymology*
chemical_list: D004279:DNA, Viral; D010450:Endopeptidases
vernacular_title: Vydelenie i ochistka 3C-proteinazy virusa poliomielita. Identifikatsiia aktivnoĭ formy fermenta.