Publication | Open Access
Relative Affinity of Hemoglobin S and Hemoglobin A for Carbon Monoxide and Oxygen
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1974
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ImmunohematologyWhole BloodRedox BiologyOxidative StressLaboratory HematologyBioanalysisHematologyClinical ChemistryLaboratory MedicineCarbon MonoxideHealth SciencesPharmacokinetic ModelingBiochemistryHeme SignalingHeme TransportRelative AffinityHeme HomeostasisHb APharmacologyPeriodic Surface StructuresRelative Affinity ConstantsHeme DegradationPhysiologyMetabolismMedicineHemoglobin S
Abstract The relative affinity constants of hemolysates from individuals with hemoglobins A, S, or AS have been measured at 37 and 26 ° C. Observed values of all hemoglobin types were the same at both temperatures, K37 = 230, K26 = 296. Control measurements on whole blood containing Hb A gave values of K37 = 222. The small but significant difference between K37 values measured in whole blood and in hemolysates may be a result of the greater increase of MetHb in the hemolysates during the in vitro equilibration.