title: Effects of ionizing radiation on nitric oxide myoglobin. Part 2. Effects on the globin moiety.
abstract: Irradiation of nitric oxide myoglobin (NOMb) induces changes in the haem as well as protein moiety of NOMb, especially at doses of 400-800 krad. The changes in the protein include: Conformational changes, with apparent partial denaturation of globin alpha-helix as evidenced by circular dichroism. Preferential scission of the polypeptide chain and dimerization via covalent bond(s) as evidenced by SDS-polyacrylamide gel electrophoresis. Products with a spectrum of hydrodynamic volumes between those of the monomer and the dimer are also formed. The shift of NOMb pIs toward more acidic pHs (probably due to modification and/or destruction of basic amino acid residues by water radiolytic products) as evidenced by isoelectric focusing.
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005514:Food Irradiation; D005720:Gamma Rays; D005914:Globins / Q000528:radiation effects*; D007525:Isoelectric Focusing; D009211:Myoglobin / Q000031:analogs & derivatives* / Q000528:radiation effects
chemical_list: D009211:Myoglobin; C031560:myoglobin nitroxide; D005914:Globins