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.
A method for the determination of CO content in blood is described. Carbon monoxide bound to hemoglobin is released by hemolysis and reaction with K3Fe(CN)6 in a closed system. The gases liberated are then swept onto a 5 A molecular sieve column where CO is separated from other blood gases. The CO, after catalytic reduction to methane, is detected by flame ionization. The method is rapid, specific, and sufficiently sensitive to permit analysis of 0.1-ml. samples of normal blood. The accuracy of the method, expressed as the coefficient of variation (S.D. x 100/mean), is 1.8% for normal human blood.
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