title: Diminishing of aggregation for bovine liver catalase through acidic residues modification.
abstract: The tendency of proteins to aggregate is an important problem in biotechnology and the pharmaceutical industry. Because proteins in the aggregated state generally do not have the same biological activity as proteins in the native state. In order to prevent aggregation, it is essential to know the effective parameters in anti-aggregation mechanism. Using a chemical protein modification approach, UV-vis and fluorescence spectroscopies and circular dichroism spectropolarimetry, this study investigates the parameters involved in anti-aggregation mechanism of bovine liver catalase. Our findings clearly indicate that the modified bovine liver catalase provides better protection than the native enzyme against thermal aggregation. It seems that a decrease in hydrophobicity resulting in chemical modification plays an important role in preventing aggregation.
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors.forename: S
authors.initials: S
authors.lastname: Hashemnia
authors.forename: A A
authors.initials: AA
authors.lastname: Moosavi-Movahedi
authors.forename: H
authors.initials: H
authors.lastname: Ghourchian
authors.forename: F
authors.initials: F
authors.lastname: Ahmad
authors.forename: G H
authors.initials: GH
authors.lastname: Hakimelahi
authors.forename: A A
authors.initials: AA
authors.lastname: Saboury
mesh_terms: D000818:Animals; D002374:Catalase / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D008958:Models, Molecular; D046912:Multiprotein Complexes; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry
chemical_list: D046912:Multiprotein Complexes; D002374:Catalase