Open AccessVariability of the magnetic moment of carbon monoxide hemoglobin from carp.
Author(s) -
M. Cerdonio,
Silvia Morante,
S. Vitale,
Alice De Young,
Robert W. Noble
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.3.1462
Subject(s) - carbon monoxide , carp , hydroxymethyl , hemoglobin , chemistry , tris , methemoglobin , inorganic chemistry , paramagnetism , nuclear chemistry , biochemistry , organic chemistry , fishery , fish <actinopterygii> , biology , catalysis , physics , quantum mechanics
Deionized carp carbon monoxide hemoglobin 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 the addition of inositol hexaphosphate to this protein in the former buffer at pH 6.3-6.4. No such effect is seen when inositol hexaphosphate is added to carp cyanomethemoglobin, demonstrating that the change observed with carbon monoxide derivative is not due to a modification in the diamagnetic properties of the protein.