title: [Renaturation of bacterial metalloproteinases].
abstract: After denaturation by phenol or acid ethanol bacterial metalloproteinases secreted by Bacillus thermoproteolyticus and Bacillus megaterium cells can be renatured by dissolution in 99.7% formic acid with subsequent dilution of the solution and its neutralization with an appropriate amount of an alkali. Renaturation is optimal at pH 9.0 in the presence of 30% glycerol as stabilizer, Ca2+ and Zn2+ ions needed for the formation of a native structure and reconstitution of the enzyme catalytic center. The active enzyme yield is 60-80%. Reactivated metalloproteinases retain their enzymatic properties, amino acid composition and molecular mass. Under these conditions autolysis of metalloproteinases does not significantly influence their renaturation.
authors.forename: T I
authors.initials: TI
authors.lastname: Vaganova
authors.forename: N P
authors.initials: NP
authors.lastname: Medvedeva
authors.forename: V M
authors.initials: VM
authors.lastname: Stepanov
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000201:enzymology*; D001410:Bacillus megaterium / Q000201:enzymology*; D002118:Calcium / Q000378:metabolism; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D013379:Substrate Specificity; D015032:Zinc / Q000378:metabolism
chemical_list: D000596:Amino Acids; D008666:Metalloendopeptidases; D015032:Zinc; D002118:Calcium
vernacular_title: Renaturatsiia bakterial'nykh metalloproteinaz.