Properties of hemoglobin a and hemoglobin Zurich (β63 histidine→arginine): Quantitative evaluation of functional abnormalities in hemoglobins
1976; Elsevier BV; Volume: 68; Issue: 4 Linguagem: Inglês
10.1016/0006-291x(76)90348-x
ISSN1090-2104
AutoresWilliam Wallace, John A. Volpe, John C. Maxwell, Winslow S. Caughey, Samuel Charache,
Tópico(s)Heme Oxygenase-1 and Carbon Monoxide
ResumoThe abnormal hemoglobin Zurich (β63 his→arg) exhibits abnormal properties. Thus, νCO occurs at 1951 cm−1 for HbACO while HbZCO shows bands at 1950 cm−1 and 1958 cm−1 for CO bound in α and β chains respectively (the βCOs are displaced less readily by O2). Acid catalyzed reductive displacement of superoxide by azide is slower on the β chain of HbZO2 than on the α chain under conditions where with HbAO2 both chains appear equally reactive. The one electron donor hydroquinone produces metHb and peroxide more rapidly from HbZO2 than from HbAO2. These property differences can be related to the β63 residue. Such studies provide generally useful probes of the structural basis for hemoglobin diseases.
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