The Multiple Functions of Hemoglobin

References

• Achilles W., Cumme G. A., Winnefeld K., Frunder H. Binding of magnesium and chloride ions to human hemoglobin A. Mg2+ concentrations in solutions simulating red cell conditions. Eur. J. Biochem. 1981; 120: 571–576
   PubMedGoogle Scholar
• Antonini E., Brunori M. Hemoglobin and Myoglobin in Their Reactions with Ligands. North-Holland Frontiers of Biology, A. Neuberger, E. L. Tatum. North-Holland, Amsterdam 1977; Vol. 21: 178–187
   Google Scholar
• Antonini E., Brunori M., Wyman J. Studies on the oxidation-reduction potentials of heme protein. IV. The kinetics of oxidation of hemoglobin and myoglobin by femcyanide. Biochemistry 1965; 4: 545–551
   PubMed Web of Science ®Google Scholar
• Bennett V. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu. Rev. Biochem. 1985; 54: 273–304
   PubMed Web of Science ®Google Scholar
• Berger H., Jänig G., Gerber G., Ruckpaul K., Rapoport S. M. Interaction of hemoglobin with ion. Interaction among magnesium, adenosine 5′-triphosphate, 2,3-biphosphoglycerate, and oxygenated and deoxygenated human haemoglobin under simulated intracellular conditions. Eur J. Biochem 1973; 38: 553–562
   PubMedGoogle Scholar
• Bienzle U., Guggenmoos-Holsmann I., Luzzatto L. Malaria and erythrocytes glucose-6-phosphate dehydrogenase variants in West Africa. Am. J. Trop. Med. Hyg. 1979; 28: 619–621
   PubMed Web of Science ®Google Scholar
• Blake C. Exons and the evolution of proteins. Trends Biochem. Sci. 1983; 8: 11–13
   Web of Science ®Google Scholar
• Blisard K. S., Mieyal J. J. Characterization of the aniline hydroxylase activity of erythrocytes. J. Biol. Chem. 1979; 254: 5104–5110
   PubMed Web of Science ®Google Scholar
• Blisard K. S., Mieyal J. J. Differential monooxygenase-like activity of fetal and adult erythrocytes. Biochem. Biophys. Res. Commun. 1980; 96: 1261–1266
   PubMed Web of Science ®Google Scholar
• Blisard K. S., Mieyal J. J. Role of NADPH and the NADPH-dependent methemoglobin reductase in the hydroxylase activity of human erythrocytes. Arch. Biochem. Biophys. 1981; 210: 762–769
   PubMed Web of Science ®Google Scholar
• Brantl V., Gramsch C., Lottspeich F., Mertz R., Jaeger K., Herz A. Novel opioid peptides derived from hemoglobin: hemorphins. Eur. J. Pharmacol. 1986; 125: 309–310
   PubMed Web of Science ®Google Scholar
• Brüne B., Ullrich V. Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol. Pharmacol. 1987; 32: 497–504
   PubMed Web of Science ®Google Scholar
• Brunori M., Falcioni G., Fioretti E., Giardina B., Rotilio G. Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation. Eur. J. Biochem. 1975; 53: 99–104
   Google Scholar
• Brunori M., Giardina B., Bannister J. V. Oxygen transport proteins. Inorganic Biochemistry (Series) 1, H. A. O. Hill. Royal Society of Chemistry, Burlington House, London 1977; 159–209
   Google Scholar
• Brunori M., Giardina B., Kuiper H. A. Oxygen transport proteins. Inorganic Biochemistry (Series) 3, H. A. O. Hill. Royal Society of Chemistry, Burlington House, London 1980; 126–182
   Google Scholar
• Bunn H. F., Ransil B. J., Chao A. The interaction between erythrocyte organic phosphates, magnesium ion, and hemoglobin. J. Biol. Chem. 1971; 246: 5273–5279
   PubMed Web of Science ®Google Scholar
• Cirsky J., Castagnola M., Amiconi G., Michalkova D. Studium der interaktion des Glykohämoglobins mit Membranen der Erythrozyten. Proc. VIII Internationales Donau-Symposium Über Diabetes Mellitus, Bratislava, 1985; 103
   Google Scholar
• Chasis J., Mohandas N. Erythrocyte membrane deformability and stability. Two distinct membrane properties that are independently regulated by skeletal protein associations. J. Cell. Biol. 1986; 103: 345–350
   Web of Science ®Google Scholar
• Cruse I., Maines M. D. Evidence suggesting the two forms of heme oxygenase are products of different genes. J. Biol. Chem. 1988; 263: 3348–3353
   PubMed Web of Science ®Google Scholar
• Clementi M. E., Condò S. G., Castagnola M., Giardina B. Hemoglobin function under extreme life conditions. Eur. J. Biochem. 1994; 223: 309–317
   PubMedGoogle Scholar
• Davis T. P., Gillespie T. J., Porreca F. Peptide fragments derived from the β-chain of hemoglobin (hemorphins) are centrally active in vivo. Peptides 1989; 10: 747–751
   PubMed Web of Science ®Google Scholar
• Devogel M., Léonis J., Vincentelli J. The alteration of the functional properties of human haemoglobin by spectrin. Experientia 1977; 33: 1429–1430
   PubMedGoogle Scholar
• di Prisco G., Condò S. G., Tamburrini M., Giardina B. Oxygen transport in extreme environments. Trends Biochem. Sci. 1991; 16: 471–474
   PubMed Web of Science ®Google Scholar
• Eaton W. The relationship between coding sequences and function in hemoglobin. Nature 1980; 284: 183–184
   PubMed Web of Science ®Google Scholar
• Eckert K. G., Eyer P. Differences in the reactions of isomeric ortho-para-aminophenols with hemoglobin. Biochem. Pharmacol. 1983; 32: 1019–1027
   PubMed Web of Science ®Google Scholar
• Elbaum D., Nagel R. L. Esterase activity of hemoglobin. Differences between HbA and HbS. J. Biol. Chem. 1981; 256: 2280–2283
   PubMed Web of Science ®Google Scholar
• Fairbanks G., Steck T. L., Wallach D. F. H. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971; 10: 2606–2617
   PubMed Web of Science ®Google Scholar
• Fermi G., Perutz M., Shanaan B., Fourne R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 1984; 175: 159–174
   PubMed Web of Science ®Google Scholar
• Ferraiolo B. L., Onady G. M., Mieyal J. J. Monooxygenase activity of human hemoglobin. Role of quaternary structure in the preponderant activity of the β subunits within the tetramer. Biochemistry 1984; 23: 5528–5534
   PubMed Web of Science ®Google Scholar
• Fortier N., Snyder M. L., Garver F., Kiefer C., McKenney J., Mohandas N. The relationship between in vivo generated hemoglobin skeletal protein complex and increased red cell membrane rigidity. Blood 1988; 71: 1427–1431
   PubMed Web of Science ®Google Scholar
• Friedman M. J. Oxidant damage mediates variant red cell resistance to malaria. Nature 1979; 280: 245–247
   PubMed Web of Science ®Google Scholar
• Giardina B., Corda M., Pellegrini M. G., Condò S. G., Brunori M. Functional properties of the hemoglobin system of two diving birds (Podiceps n.Phalacrocorax c.s.). Mol. Physiol. 1985; 7: 281–292
   Google Scholar
• Giardina B., Corda M., Pellegrini M. G., Sanna M. T., Brix O., Clementi M. E., Condò S. G. Flight and heat dissipation in birds: a possible molecular mechanism. FEBS Lett. 1990; 270: 173–176
   PubMed Web of Science ®Google Scholar
• Giardina B., Scatena R., Clementi M. E., Cerroni L., Nuutinen M., Brix O., Sletten S. N., Castagnola M., Condò S. G. Physiological relevance of the overall δH of oxygen binding to fetal human hemoglobin. J. Mol. Biol. 1993; 229: 512–516
   PubMed Web of Science ®Google Scholar
• Giardina B., Scatena R., Clementi M. E., Ramacci M. T., Maccari F., Cerroni L., Condò S. G. Selective binding of met-hemoglobin to erythrocytic membrane: a possible involvement in red blood cell aging. Red Blood Cell Aging, M. Magnani, A. De Flora. Plenum Press, New York 1991; 75–84
   Google Scholar
• Giuliani A., Marini S., Ferroni L., Condò S. G., Ramacci M. T., Giardina B. Anion exchange protein (band 3) in human erythrocytes characterized by different abnormalities. Clin. Chim. Acta 1993; 220: 211–217
   PubMed Web of Science ®Google Scholar
• Hamasaki N., Asakura T., Minakami S. Effect of oxygen tension on glyco-lysis in human erythrocytes. J. Biochem. (Tokyo) 1970; 68: 157–161
   PubMed Web of Science ®Google Scholar
• Harris S. J., Winzor D. J. Interactions of glycolytic enzymes with erythro-cyte membranes. Biochim. Biophys. Acta 1990; 1038: 306–314
   PubMedGoogle Scholar
• Hebbel R. P. Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology. Blood 1991; 77: 214–237
   PubMed Web of Science ®Google Scholar
• Hebbel R. P., Morgan W. T., Eaton J. W., Hedlund B. E. Accelerated auto-oxidation and heme loss due to the instability of sickle hemoglobin. Proc. Natl. Acad. Sci. U. S. A. 1988; 85: 237–241
   PubMed Web of Science ®Google Scholar
• Higashi R., Richards C. S., Uyeda K. The interaction of phosphofructoki-nase with erythrocyte membrane. J. Biol. Chem. 1979; 254: 9542–9550
   PubMed Web of Science ®Google Scholar
• Hirst D. J., Wood P. J. Could manipulation of the binding affinity of hemoglobin for oxygen be used clinically to sensitize tumours to radiation. Radiother. Oncol. 1991; 20: 53–57
   PubMed Web of Science ®Google Scholar
• Jacob H. S., Brain M. C., Dacie J. V. Altered sulfhydryl reactivity of hemoglobins and red blood cell membranes in congenital Heinz body hemolytic anemia. J. Clin. Invest. 1968; 47: 2664–2677
   PubMed Web of Science ®Google Scholar
• Jay D., Cantley L. Structural aspects of the red cell anion exchange protein. Annu. Rev. Biochem. 1986; 55: 511–538
   PubMed Web of Science ®Google Scholar
• Jenkins J. D., Kezdy F. J., Steck T. L. Mode of interaction of phospho-fructokinase with the erythrocyte membrane. J. Biol. Chem. 1985; 260: 10426–10433
   PubMed Web of Science ®Google Scholar
• Juchau M. R., Simms K. G. Aniline hydroxylation in the human placenta: mechanistic aspect. Biochem. Pharmacol. 1972; 21: 2053–2064
   PubMed Web of Science ®Google Scholar
• Khoo U. Y., Mewman D. J., Miller W. K., Price C. P. The influence of glycation on the peroxidase activity of haemoglobin. Eur. J. Clin. Chem. Clin. Biochem. 1994; 32: 435–440
   PubMedGoogle Scholar
• Kliman H. J., Steck T. L. Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. J. Biol. Chem. 1980; 255: 6314–6321
   PubMed Web of Science ®Google Scholar
• Klipstein F. A., Ranney H. M. Electrophoretic components of the hemoglobin of red cell membranes. J. Clin. Invest. 1960; 39: 1894–1899
   PubMed Web of Science ®Google Scholar
• Lantz I., Glhsta E. L., Talbäck L., Nyberg F. Hemorphins derived from hemoglobin have an inhibitory on angiotensin converting enzyme activity. FEBS Lett. 1991; 287: 39–41
   PubMed Web of Science ®Google Scholar
• Lebbar I., Stetzkowski-Marden F., Mauffret O., Cassoly R. Interaction of actin and tubulin with human deoxy-hemoglobin. Their possible occurrence within the erythrocytes. Eur. J. Biochem. 1987; 170: 273–277
   PubMedGoogle Scholar
• Liddington R., Derewenda Z., Dodson E., Hubbard R., Dodson G. High resolution crystal structure and comparison of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(α-oxy) haemoglobin and T(met)haemoglobin. J. Mol. Biol. 1992; 228: 551–579
   PubMed Web of Science ®Google Scholar
• Lin H., McGrath J. J. Carbon monoxide effects on calcium levels in vascular smooth muscle. Life Sci. 1988; 43: 1813–1816
   PubMed Web of Science ®Google Scholar
• Low P. S. Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane-peripheral protein interaction. Biochim. Biophys. Acta 1986; 864: 145–167
   PubMed Web of Science ®Google Scholar
• Low P. S. Role of hemoglobin denatur-ation and band 3 clustering initiating red cell removal. Red Blood Cell Aging, M. Magnani, A. De Flora. Plenum Press, New York 1991; 173–183
   Google Scholar
• Low P. S., Rathinavelu P., Harrison M. L. Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3. J. Biol. Chem. 1993; 268: 14627–14631
   PubMed Web of Science ®Google Scholar
• Low P. S., Waugh S. M., Zinke K., Drenckhahn D. The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 1985; 227: 531–533
   PubMed Web of Science ®Google Scholar
• Lutz P. L. On the oxygen affinity of bird blood. Am. Zool. 1980; 20: 187–198
   Google Scholar
• Luzzatto L., Nwachukes-Jarrett E. S., Reddy S. Increased sickling of parasitized erythrocytes as mechanisms of tesistance against malaria in sickle cell trait. Lancet 1970; 1: 319–321
   PubMed Web of Science ®Google Scholar
• Mairbaurl H., Oelz O., Bärtsch P. Interactions between Hb, Mg, DPG, ATP, and C1 determine the change in Hb-O2 affinity at high altitude. J. Appl. Physiol. 1993; 74: 40–48
   PubMed Web of Science ®Google Scholar
• Mansouri A., Perry C. A. Alteration of platelet aggregation by cigarette smoke and carbon monoxide. Thromb. Haemost. 1982; 48: 286–288
   PubMed Web of Science ®Google Scholar
• Mansouri A., Perry C. A. Inhibition of platelet ADP and serotonine release by carbon monoxide and cigarette smokers. Experientia 1983; 40: 515–517
   Google Scholar
• Mansouri A., Winterhalter K. H. Non-equivalence of chains in hemoglobin oxidation and oxygen binding. Effect of organic phosphates. Biochemistry 1974; 13: 3311–3314
   PubMed Web of Science ®Google Scholar
• Marks G. S., Bnen J. F., Nakatsu K., McLaughlin B. E. Does carbon monoxide have a physiological function. Trends Pharm. Sci. 1991; 12: 185–188
   PubMed Web of Science ®Google Scholar
• McPherson R. A., Sawyer W. H., Tilley L. Rotational diffusion of the eryth-rocyte integral membrane protein band 3: effect of hemichrome binding. Biochemistry 1992; 31: 512–518
   PubMed Web of Science ®Google Scholar
• Mohandas N., Chasis J., Shohet S. The influence of the membrane skeleton on red cell defonmability, membrane material properties and shape. Semin. Hematol. 1983; 20: 225–242
   PubMed Web of Science ®Google Scholar
• Monod J., Wyman J., Changeux J. P. On the nature of allosteric transition: a plausible model. J. Mol. Biol. 1965; 12: 88–118
   PubMed Web of Science ®Google Scholar
• Mob de Freitas D., Amari L., Srinivasan C., Rong Q., Ramasamy R., Abraha A., Geraldes C. F. G. C., Boyd M. K. Competition between Li' and Mg++ for the phosphate groups in the human erythrocyte membrane and ATP: an NMR and fluorescence study. Biochemistry 1994; 33: 4101410
   Web of Science ®Google Scholar
• Murthy S. N. P., Kaul R. K., Köhler H. Hemoglobin binds to the amino-terminal 23-residue fragment of human erythrocyte band 3 protein. Hoppe-Seyler's Z. Physiol. Chem. 1984; 365: 9–17
   PubMedGoogle Scholar
• Murthy S. N. P., Liu T., Kaul R. K., Köhler H., Steck T. L. 1981, The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band
   Google Scholar
• Murthy S. N. P., Liu T., Kaul R. K., Köhler H., Steck T. L. The aldolasebinding site of the human ertthrocyte membrane is at the NH2 terminus of band 3. J. Bid. Chem. 1981; 256: 11203–11208
   PubMed Web of Science ®Google Scholar
• Nagel R. L., Roth E. F., Jr. Malaria and red cell genetic defects. Blood 1989; 74: 1213–1221
   PubMed Web of Science ®Google Scholar
• Orjih A. U., Fitch C. D. Hemozoin production by Plasmodium falciparum: variation with strain and exposure to chloroquine. Biochim. Biophys. Acta 1993; 1157: 270–274
   PubMed Web of Science ®Google Scholar
• Perrella M., Shrager R. I., Ripamonti M., Manfredi G., Berger R. L., Rossi-Bernardi L. Mechanism of the oxidation reaction of deoxyhemoglobin as studied by isolation of the intermediates suggests tertiary structure dependent cooperativity. Biochemistry 1993; 32: 5233–5238
   PubMed Web of Science ®Google Scholar
• Pert C. B., Pert A., Tallmann J. F. Isolation of a novel endogenous opiate analgesic from human blood. Proc. Natl. Acad. Sci. USA 1976; 73: 2226–2230
   PubMed Web of Science ®Google Scholar
• Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature 1970; 228: 726739
   Web of Science ®Google Scholar
• Perutz M. F., Kilmartin J. V., Nishikura K., Fogg J. H., Butler P. J. G., Rollema H. S. Identification of residues contributing to the Bohr effect of human hemoglobin. J. Mol. Biol. 1980; 138: 649–670
   PubMed Web of Science ®Google Scholar
• Piot J. M., Zhao Q., Guillochon D., Ricart G., Thomas D. Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydroly-sate. Biochem. Biophys. Res. Commun. 1992; 189: 101–110
   PubMed Web of Science ®Google Scholar
• Rachmilewitz E. A., Peisach J., Blumberg W. E. Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives. J. Biol. Chem. 1971; 246: 3356–3366
   PubMed Web of Science ®Google Scholar
• Ramos K. S., Lin H., McGrath J. J. Modulation of cyclic guanosine monophosphate levels in cultured aortic smooth muscle cells by carbon monoxide. Biochem. Pharmacol. 1989; 38: 1368–1370
   PubMed Web of Science ®Google Scholar
• Rapoport I., Berger H., Rapoport S. M., Elsner R., Gerber G. Response of the glycolysis of human erythrocytes to the transition from the oxygenated to the deoxygenated state at constant intra-cellular pH. Biochim. Biophys. Acta 1976; 428: 193–204
   PubMedGoogle Scholar
• Riggs A. F. The Bohr effect. Annu. Rev. Physiol. 1988; 50: 181–204
   PubMed Web of Science ®Google Scholar
• Roth E. F., Jr., Friedman M., Ueda Y., Tellez I., Trager W., Nagel R. L. Sickling rates of human AS red cells infected in vitro with Plasmodium falciparum malaria. Science 1978; 202: 650–652
   PubMed Web of Science ®Google Scholar
• Roth E. F., Jr., Schulman S., Vanderberg J., Olson J. Pathways for the reduction of oxidized glutathione in the Plasmodium falciparum-infected eryth-rocyte: can parasite enzymes replace host red cell glucose-6-phosphate dehydroge-nase. Blood 1986; 67: 827–830
   PubMed Web of Science ®Google Scholar
• Sadrzadeh S. M. H., Graf E., Panter S. S., Hallaway P. E., Eaton I. W. Hemoglobin. A biologic Fenton reagent. J. Biol. Chem. 1984; 259: 14356–14356
   Web of Science ®Google Scholar
• Salhany J. M., Cassoly R. Kinetics of p-mercurybenzoate binding of sulfhy-dry1 groups on the isolated cytoplasmic fragment of band 3 protein. J. Biol. Chem. 1989; 265: 1399–1404
   Google Scholar
• San George R. C., Nagel R. L., Fabry M. E. On the mechanism for red-cell accumulation of mefloquine, an antimalarial drug. Biochim. Biophys. Acta 1984; 803: 174–181
   PubMed Web of Science ®Google Scholar
• Sayare M., Fikiet M. Cross-linking of hemoglobin to the cytoplasmic surface of human erythrocyte membranes. J. Biol. Chem. 1981; 256: 13152–13158
   PubMed Web of Science ®Google Scholar
• Scatena R., Nocca G., Messana I., De Sole P., Baroni S., Zuppi C., Castagnola M., Giardina B. Effects of gem-fibrozil on the oxygen transport properties of erythrocytes. Br. J. Clin. Pharmacol. 1995; 39: 25–30
   PubMed Web of Science ®Google Scholar
• Schluter K., Drenckhahn D. Co-clustering of denatured haemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc. Natl. Acad. Sci. U. S. A. 1986; 83: 6137–6141
   PubMed Web of Science ®Google Scholar
• Shaanan B. Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 1983; 171: 31–59
   PubMed Web of Science ®Google Scholar
• Siemann D. W., Alliet K. L., Macler L. M. Manipulations in the oxygen transport capacity of blood as a means of sensitizing tumors to radiation therapy. Int. J. Radiat. Oncol. Biol. Phys. 1989; 16: 1169–1172
   PubMed Web of Science ®Google Scholar
• Simoes A. P., van den Berg J. J. M., Roelopsen B., Op den Kamp J. A. F. Lipid peroxidation in Plasmodium falciparum-parasitized human erythrocytes. Arch. Biochem. Biophys. 1992; 298: 651–657
   PubMed Web of Science ®Google Scholar
• Starke D. W., Blisard K. S., Mieyal J. J. Substrate specificity of the mono-oxygenase activity of hemoglobin. Mol. Pharmacol. 1984; 25: 467475
   Web of Science ®Google Scholar
• Stocker R., Yamamoto Y., McDonagh A. F., Glazer A. N., Ames B. N. Bilirubin is an antioxidant of possible physiological importance. Science 1987; 235: 1043–1046
   PubMed Web of Science ®Google Scholar
• Strapazon E., Steck T. L. Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membrane. Biochemistry 1976; 15: 1421–1424
   PubMed Web of Science ®Google Scholar
• Tilley L., Foley M., Anders R. F., Dluzewski A. R., Gratzer W. B., Jones G. L., Sawyer W. H. Rotational dynamics of the integral membrane protein band 3, as a probe of the membrane events associated with Plasmodium falciparum infections of human erythrocytes. Biochim. Biophys. Acta 1990; 1025: 135–142
   PubMedGoogle Scholar
• Tomita S. Modulation of the oxygen equilibria of human foetal and adult hemoglobins by 2,3-diphosphoglyceric acid. J. Biol. Chem. 1981; 256: 9495–9500
   PubMed Web of Science ®Google Scholar
• Tomoda A., Hamashima H., Arisawa M., Kikuchi T., Tezuka Y., Koshimura S. Phenoxazinone synthesis by human hemoglobin. Biochim. Biophys. Acta 1992; 1117: 306–314
   PubMedGoogle Scholar
• Tomoda A., Shirasawa E., Nagao S., Minami M., Yoneyama Y. Involvement of oxidoreductive reactions of intracellular haemoglobin in the metabolism of 3-hydroxyantranilic acid in human erythrocyte. Biochem. J. 1984; 222: 755–760
   PubMed Web of Science ®Google Scholar
• Tomoda A., Takeshita M., Yoneyama Y. Analysis of met-form hemoglobin in glucose-depleted human red cells. FEBS Lett. 1978; 88: 247–251
   PubMed Web of Science ®Google Scholar
• Tomoda A., Yamaguchi J., Kojima H., Amemiya H., Yoneyama Y. Mechanism of o-aminophenol metabolism in human erythrocytes. FEBS Lett. 1986; 196: 44–48
   PubMed Web of Science ®Google Scholar
• Usanga E. A., Luzzatto L. Adaptation of Plasmodium falciparum to glucose 6-phosphate dehydrogenase-deficient host red cells by production of parasite-encoded enzyme. Nature 1985; 313: 793–795
   PubMed Web of Science ®Google Scholar
• Utz J., Ullrich V. Carbon monoxide relaxes ileal smooth muscle through activation of guanylate cyclase. Biochem. Pharmacol. 1991; 41: 1195–1201
   PubMed Web of Science ®Google Scholar
• Vedernikov Y. P., Gräser T., Vanin A. F. Similar endothelium-independent arterial relaxation by carbon monoxide and nitric oxide. Biomed. Biochim. Acta 1989; 48: 601–603
   PubMedGoogle Scholar
• Walder J. A., Chattejee R., Steck T. L., Low P. S., Musso G. F., Kaiser E. T., Rogers P. H., Amone A. The interaction of hemoglobin with the cyto-plasmic domain of band 3 of human erythrocyte membrane. J. Bid. Chem. 1984; 259: 10238–10246
   PubMed Web of Science ®Google Scholar
• Wang D. N., Kühlbrandt W., Sarabia V. E., Reithmeier R. A. F. Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO J. 1993; 12: 2233–2239
   PubMed Web of Science ®Google Scholar
• Waugh S. M., Low P. S. Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane. Biochemistry 1985; 24: 34–39
   PubMed Web of Science ®Google Scholar
• Weber R. E., Jensen F. B. Functional adaptation in hemoglobins from ectothermic vertebrates. Annu. Rev. Physiol. 1988; 50: 161–179
   PubMed Web of Science ®Google Scholar
• Weber R. E., Wells R. M. G. Hemoglobin structure and function. Comparative Pulmonary Physiology. Current Concepts, S. C. Wood. Marcel Dekker, New York 1989; Vol. 39: 279–310
   Google Scholar
• Wiedenmann B., Elbaum D. Effect of hemoglobin A and S on human erythrocyte ghosts. J. Biol. Chem. 1983; 258: 5483–5489
   PubMed Web of Science ®Google Scholar