Variability of the magnetic moment of carbon monoxide hemoglobin from carp.

Abstract

Deionized carp HbCO in distilled water or in bis(2-hydroxyethyl)imino-tris(hydroxymethyl)methane or Tris buffer exhibits a slight but significant paramagnetism. This is most clearly demonstrated by the decrease in this paramagnetism that is caused by addition of inositol hexaphosphate [IHP] to this protein in the former buffer at pH 6.3-6.4. No such effect is seen when IHP is added to carp cyanomethemoglobin, demonstrating that the change observed with the CO derivative is not due to a modification in the diamagnetic properties of the protein.