title: Horseradish peroxidase renaturation is less efficient at lower protein concentrations.
abstract: Renaturation of horseradish peroxidase from guainidine hydrochloride has been studied. Although refolding of the secondary structure was complete, only partial heme incorporation and recovery of enzymatic activity were observed. Heme capturing became less efficient at lower peroxidase concentrations: the refolding yield decreased from 60% at 1 microM to 10% at 0.1 microM concentration of the protein. Probing with conformation-sensitive antibodies indicated structural differences between peroxidase refolded at low concentration and the holo-enzyme.
authors.affiliation: Institute of Biochemistry, Russian Academy of Sciences, Leninsky prospect 33, 119071 Moscow, Russia.
authors.forename: D N
authors.initials: DN
authors.lastname: Ermolenko
authors.forename: A V
authors.initials: AV
authors.lastname: Zherdev
authors.forename: B B
authors.initials: BB
authors.lastname: Dzantiev
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D004797:Enzyme-Linked Immunosorbent Assay; D006418:Heme / Q000378:metabolism; D020035:Holoenzymes / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects
chemical_list: D020035:Holoenzymes; D006418:Heme; D006735:Horseradish Peroxidase