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Oxygen Equilibrium of Hemoglobin E

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Oxygen Equilibrium of Hemoglobin E Oxygen equilibrium of hemoglobin E H. Franklin Bunn, … , Stanley P. Balcerzak, Donald L. Rucknagel J Clin Invest. 1972;51(11):2984-2987. https://doi.org/10.1172/JCI107125. Concise Publication Oxygen equilibrium was determined on hemoglobin of individuals both heterozygous and homozygous for hemoglobin E. The whole blood oxyhemoglobin dissociation curve of AE blood was identical to that of normal AA blood. E hemoglobin, isolated by diethylaminoethyl Sephadex and carboxymethyl cellulose column chromatography, had oxygen affinity, heme- heme interaction, and Bohr effect identical to those of hemoglobin A prepared from the same column. Furthermore, the two hemoglobins had equal reactivity with 2,3-diphosphoglycerate. Phosphate-free hemolysates of blood from E and A homozygotes also had identical oxygen saturation curves. These results do not confirm earlier reports that hemoglobin E has an abnormally low oxygen affinity. Find the latest version: https://jci.me/107125/pdf Oxygen Equilibrium of Hemoglobin E H. FRANKLIN BUNN, W. DELANO MERIWETHER, STANLEY P. BALCERZAK, and DONALD L. RUCKNAGEL From the Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118 and the Harvard Medical School, Boston, Massachusetts 02115; the Department of Medicine, Ohio State University, Columbus, Ohio 43210; and the Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105 A B S T R A C T Oxygen equilibrium was determined on METHODS hemoglobin of individuals both heterozygous and ho- Blood was obtained from a 32-yr old Thai male homozygous mozygous for hemoglobin E. The whole blood oxyhemo- for hemoglobin E. His hemoglobin concentration was 15.6 globin dissociation curve of AE blood was identical to g/100 ml; hematocrit was 44.2%. Slight anisocytosis, poi- that of normal AA blood. E hemoglobin, isolated by kilocytosis, and many target cells were noted on the stained peripheral blood film. Cellulose acetate electrophoresis diethylaminoethyl Sephadex and carboxymethyl cellu- showed only hemoglobin E as the major component. Hemo- lose column chromatography, had oxygen affinity, heme- globin F comprised 0.9%o of the total as measured by alkali heme interaction, and Bohr effect identical to those of denaturation. A sample of this individual's blood was air- hemoglobin A prepared from the same column. Fur- mailed in acid citrate dextrose and on ice for oxygen thermore, the two hemoglobins had equal reactivity with equilibrium measurements. Blood was also obtained from an American Black male heterozygous for hemoglobin E. 2,3-diphosphoglycerate. Phosphate-free hemolysates of The structure of the E hemoglobin from each donor was blood from E and A homozygotes also had identical oxy- verified by two-dimensional peptide mapping (9) of the gen saturation curves. These results do not confirm ear- variant polypeptide chains isolated by the column chromato- lier reports that hemoglobin E has an abnormally low graphic method of Clegg, Naughton, and Weatherall (10). The abnormal tryptic peptides were eluted from the paper oxygen affinity. chromatogram and the composition verified on a Beckman Automatic Amino Acid Analyser 120C (Beckman Instru- ments, Inc., Palo Alto, Calif.). INTRODUCTION Phosphate-free hemoglobin solutions and a standard solu- Functional studies of certain abnormal human hemoglo- tion of 2,3-diphosphoglycerate (2,3-DPG) 1 were prepared as described previously (11). From a hemolysate of the bins have provided valuable information on the mecha- heterozygote, A and E hemoglobins were separated by nism by which ligands, such as oxygen, bind to hemo- two types of ion exchange chromatography: diethylamino- globin. Most hemoglobin variants having increased oxy- ethyl Sephadex (DEAE-Sephadex) (12) and carboxy- gen affinity have amino acid substitutions in regions of methyl cellulose (CM-cellulose) (13). Hemoglobin E mi- grates more rapidly than A on DEAE-Sephadex. On the molecule which are considered vital to its function CM-cellulose, the reverse is true. Hemoglobin E comprised (1). Several recent reviews have listed hemoglobin E about 35% of the total. Auto-oxidation of hemoglobins on (a2,826gI U1Y) among the hemoglobin variants that have the CM-cellulose column was prevented by equilibrating abnormally low oxygen affinity (2-4). Supporting ex- the column and eluting buffer with 1 atm of carbon mon- evidence, however, is somewhat circumstantial oxide. Carboxyhemoglobin was converted to oxyhemoglobin perimental as described previously (11). The hemoglobin-rich peaks (5-8). A more detailed examination of the oxygen that were eluted from the columns were concentrated by equilibrium of hemoglobin E is warranted not only be- ultrafiltration with a Diaflo membrane.' There was no car- cause of structural-functional implications but also be- boxyhemoglobin and less than 5% methemoglobin detectable cause this hemoglobin is the third most common variant on completion of the oxygen equilibrium measurements. world-wide, and any significant alteration of its oxygen Whole blood oxygen equilibria were done on fresh hepa- affinity could have important clinical implications. 'Abbreviations used in this paper: 2,3-DPG, 2,3-diphospho- glycerate; CM-cellulose, carboxymethyl cellulose; DEAE- Received for publication. 6 July 1972 anid in revised forin Sephadex, diethylaminoethyl Sephadex. 14 August 1972. 2 Amicon Corp., Lexington, Mass. 2984 The Journal of Clinical Investigation Volume 51 November 1972 rinized specimens of AE and AA blood. 2.5-ml specimens were mixed in a rotating tonometer at 370C with hydrated 3 *^ gas mixtures consisting of known amounts of oxygen, 5% *8g A carbon dioxide, and balance nitrogen. 10-min incubation A A IA periods were sufficient to insure full equilibration. On each n 2- specimen, the oxyhemoglobin and.total hemoglobin contents were measured by a CO oximeter.' The instrument was standardized with blood treated with sodium dithionite I. (0% 02 saturation) and pure oxygen gas (100% 02 satu- 7- was at ration). pH measured anaerobically 370C.1 The 6 p02 was corrected to a standard plasma pH of 7.40 by the use of the following Bohr factor: Alog p02/ApH = - 0.48. 5 Spectrophotometric oxygen equilibrium curves were done at 20'C on 0.1 mm (tetramer) hemoglobin solution in 0.05 M 4- bis-Tris' or Tris buffer, pH 6.4-8.6 and sufficient NaCl so ion concentration was 0.10 M that the chloride (11). 3 * Red cell 2,3-DPG was measured by the method of Keitt (14). Ps (mm Hg) RESULTS 2 00 Whole blood oxygen saturation curves done simultane- A ously on AA and AE individuals are shown in Fig. 1. The two blood specimens had identical and normal oxy- gen affinities. Furthermore, each had normal red cell 2,3- DPG: AE, 4.68 mmoles/liter RBC; AA, 4.40 mmoles/ 65 70 75 8.0 liter RBC. Normal mean ±+1 SD = 4.5±0.4 mM. pH The oxygen affinities and n values of E and A hemo- FIGURE 2 Alkaline Bohr effect of isolated A and E hemo- globins isolated on the same columns are shown in Fig. globins. Below: P,, is plotted on a logarithmic scale against 2. The type of ion exchange resin and, secondarily, pH. 0.1 mm hemoglobin in 0.1 M chloride, 0.05 M Tris or bis-Tris buffer, 20°C. Above: Hill's n is plotted against pH. 100 0, hemoglobin A prepared on DEAE-Sephadex; 0, hemo- globin A prepared on CM- cellulose; A, hemoglobin E pre- pared on DEAE-Sephadex; A, hemoglobin E prepared on CM-cellulose. 80 A the length of time the hemoglobins remained on the col- A umn had no significant effect on their oxygen equilibria. Over a wide pH range, the two hemoglobins had nearly 0 identical values for P5o, the partial pressure at which the 60 were A hemoglobin solutions half-saturated. Furthermore, z 0 A and E hemoglobins had the same degree of heme-heme !a interaction (subunit cooperativity ). The calculated alka- line Bohr factor (A log P5o/A pH) for the two hemo- 40 I) globins was - 0.54, in good agreement with a value of - 0.57 obtained in this laboratory for normal phosphate- 0 04~~~~ 0 free human hemolysate. Hemoglobins A and E showed :7---. --.. identical reactivity to 0.2 mM 2,3-DPG (Table I). 20 Identical oxygen equilibria were obtained on phosphate- free hemolysates prepared from blood specimens of homozvgotes for hemoglobins A and E (Tahle I). 0 20 40 60 DISCUSSION P02 - mm Hg These data indicate that hemoglobin E has oxygen equilibria identical to that of hemoglobin A. This con- FIGURE 1 Whole blood oxygen equilibria, pH 7.40, 37° C. trasts with the results of Thompson. Warrington, and A, AE heterozygote. 0, normal (AA homozygote). Bell (5) who studied A and E hemoglobins isolated 'Instrumentation Laboratories, Inc., Lexington, Mass. from the blood of an AE heterozygote. The single pair 'General Biochemicals Div., Chagrin Falls, Ohio. of oxygen dissociation curves which they reported, Oxygen Equilibrium of Hemoglobin E 2985 TABLE I This would be true if the deoxy-conformation of hemo- Oxygen Equilibria of A and E Hemoglobins* globin E were stabilized by aggregation in a manner similar to deoxyhemoglobin S (17). Unfortunately, we A E were not able to do a whole blood oxygen saturation Experiment 2,3-DPG P60 nt P50 n4 curve on a fresh specimen from an E homozygote. How- ever, as shown in Fig. 1, the whole blood oxygen affi- mM mm Hg mm Hg nity of an AE heterozygote was normal.' It is noteworthy I§ 0 3.7 2.9 3.9 2.7 that the functionally abnormal human hemoglobin vari- 3.9 2.9 3.9 2.9 ants which have been reported to date have all appeared 0.2 7.0 2.9 7.4 2.6 in heterozygotes having abnormal whole blood oxyhemo- globin dissociation curves. Ilij 0 3.0 2.7 3.1 2.7 Morimoto, Lehmann, and Perutz (4) suggested that 0.2 6.6 2.7 6.8 2.7 the amino acid substitution in hemoglobin E might de- stabilize the oxy-conformation leading to decreased oxy- * 0.1 mui hemoglobin (tetramer) in 0.1 M NaCl, 0.05 M bis-Tris buffer, pH 7.20, 20'C.
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