Aplysia oxymyoglobin with an unusual stability property.
Native oxymyoglobin was isolated directly from the radular muscle of Aplysia kurodai with complete separation from metmyoglobin on a DEAE-cellulose column. It was examined for its spectral and stability properties. The spectrum of Aplysia MbO2 , which lacks the distal histidine, is very similar to those of mammalian oxymyoglobins , the alpha-peak being higher than the beta-peak and the absorbance ratio being 1.03. Its stability, however, is quite different from those of the mammalian oxymyoglobins , and Aplysia MbO2 is found to be extremely susceptible to autoxidation. Its rate is one-hundred times higher at pH 9.0, and its pH dependence is unusual and much less steep, when compared with sperm whale MbO2 as reference.
D000818:Animals; D001048:Aplysia / Q000032:analysis*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D006736:Horses; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008786:Metmyoglobin / Q000302:isolation & purification; D009211:Myoglobin / Q000302:isolation & purification; D013057:Spectrum Analysis; D014907:Whales
D009211:Myoglobin; C017595:oxymyoglobin; D008786:Metmyoglobin