Dyshemoglobinemias

Disorders of Hemoglobin: Genetics, Pathophysiology, and Clinical Management, Second Edition

Volumn , Issue , 2009, Pages 607-622

  Agarwal, Neeraj ^a   Nagel, Ronald L ^b   Prchal, Josef T ^c  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b Hematology Division University of Utah ^*  (United States)

^c UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84856387440     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1017/CBO9780511596582.034     Document Type: Chapter

References (177)

1. Darling R, Roughton F. The effect of methemoglobin on the equilibrium between oxygen and hemoglobin. Am J Physiol. 1942;137:56.
2. Olsen M, McEvoy GK. Methemoglobinemia induced by topical anesthetics. AmJ Hosp Pharm. 1981;38:89-93.
3. Percy MJ, McFerran NV, Lappin TR. Disorders of oxidised haemoglobin. Blood Rev. 2005;19:61-8.
4. Misra H, Fridorich I. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem. 1972;247:6960.
5. Jaffe E, Neumann, G. A comparison of the effect of mendione, methylene blue, and ascorbic acid on the reduction of methemoglobin in vivo. Nature. 1964;202:607.
6. Jaffe E, Hultquist D. Cytochrome b5 reductase deficiency and enzymopenic hereditary methemoglobinemia. In: Scriver C, Beaudet A, Sly W, Valle D, eds. The Metabolic and Molecular Bases of Inherited Disease. 7th ed., New York: Mc-Graw Hill; 1995;2:3399.
7. Feelisch M, Kubitzek, D, Werringloer, J. The oxyhemoglobin assay. In: Feelisch M, Stamler J, eds. Methods in Nitric Oxide Research; New York: JohnWiley and Sons;1996:453.
8. Stuhlmeier K, Kao, JJ, Wallbrandt P, et al. Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates. Eur J Biochem. 2003;270:334-41.
9. Strittmatter P. The reaction sequence in electron transfer in the reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase system. J Biol Chem. 1965;240:4481.
10. Iyanagi T, Watanabe, S, Anan, KF. One-electron oxidationreduction properties of hepatic NADH-cytochrome b5 reductase. Biochemistry. 1984;23:1418-25.
11. Scott EM, Mc GJ. Purification and properties of diphosphopyridine nucleotide diaphorase of human erythrocytes. J Biol Chem. 1962;237:249-52.
12. Kuma F, Ishizawa S, Hirayama K, et al. Studies on methemoglobin reductase. I. Comparative studies of diaphorases from normal and methemoglobinemic erythrocytes. J Biol Chem. 1972;247:550.
13. Passon P, Hultquist D. Soluble cytochrome b5 reductase from human erythrocytes. Biochim Biophys Acta. 1972;275: 62.
14. Hackett C, Strittmatter P. Covalent cross-linking of the active sites of vesicle-bound cytochrome b5 and NADHcytochrome b5 reductase. J Biol Chem. 1984;259:3275.
15. Warburg O, Kubowitz F, Christian W. Uber die katalytische wirkung von methlenblau in lebenden zellen. Biochem Z. 1930;227:245.
16. Kiese M. Die reduktion des hamiglobins. 1944;316:264.
17. Yubisui T, Takeshita M, Yoneyama Y. Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. J Biochem (Tokyo). 1980;87:1715.
18. Yubisui T, Miyata T, Iwanaga S, et al. Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes. J Biochem. 1986;99:407.
19. Francois. A case of congenital cyanosis without an apparent cause. Bull Acad RoyMed Belg. 1845;4:698.
20. Hitzenberger K. Autotoxic cyanosis due to intraglobular methemoglobinemia. Wien ArchMed. 1932;23:85.
21. Gibson Q. Historical note: methemoglobinemia-long ago and far away. Am J Hematol. 1993;42:3-6.
22. Gibson Q. Introduction: congenital methemoglobinemia revisited. Blood. 2002;100:3445.
23. Percy M, Gillespie M, Savage G, et al. Familial idiopathic mutations in NADH-cytochrome b5 reductase. Blood. 2002;100:3447.
24. Bull P, Shephard E, Povey S, et al. Cloning and chromosomal mapping of human cytochrome b5 reductase (DIA1). Ann Hum Genet. 1988;52:263.
25. Tomatsu S, Kobayashi Y, Fukumaki Y, et al. The organization and the complete nucleotide sequence of the human NADHcytochrome b5 reductase gene. Gene. 1989;80:353-361.
26. Percy MJ, Oren H, Savage G, Irken G. Congenital methaemoglobinaemia Type I in a Turkish infant due to a novel mutation, Pro144Ser, inNADH-cytochrome b5 reductase.Hematol J. 2004;5(4):367-370.
27. Percy MJ, Crowley LJ, Davis CA, et al. Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase. Br J Haematol. 2005;129(6):847-853.
28. Percy MJ, Crowley LJ, Boudreaux J, et al. Expression of a novel P275L variant of NADH:cytochrome b5 reductase gives functional insight into the conserved motif important for pyridine nucleotide binding. Arch Biochem Biophys. 2006;447(1):59-67.
29. Wang Y, Wu Y, Zheng P, et al. A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. Blood. 2000; 95:3250.
30. Higasa K, Manabe J, Yubisui T, et al. Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. Br J Haematol. 1998;103:922.
31. Shotelersuk V, Tosukhowong P, Chotivitayatarakorn P, et al. A Thai boy with hereditary enzymopenic methemoglobinemia type II. JMed Assoc Thai. 2000;83:1380.
32. Jenkins M, Prchal J. A novel mutation found in the 3ʹ domain of NADH-cytochrome b5 reductase in an African-American family with type I congenital methemoglobinemia. Blood. 1996;87:2993-2999.
33. Nussenzveig R, Lingam HB, Gaikwad A, et al. A novel mutation of the cytochrome-b5 reductase gene in an Indian patient: the molecular basis of type I methemoglobinemia. Haematologica. 2006;91:1542-1545.
34. Jenkins M, Prchal J. A high frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans. Hum Genet. 1997;99:248-250.
35. Pietrini G, Carrera P, Borgese N. Two transcripts encode rat cytochrome b5 reductase. Proc Natl Acad Sci USA. 1988;85:7246-7250.
36. Pietrini G, Aggujaro D, Carrera P, et al. A single mRNA, transcribed from an alternative erythroid-specific promoter, codes for two non-myristylated forms of NADH-cytochrome b5 reductase. J Cell Biol. 1992;117:975.
37. Mota Vieira L, Kaplan J-C, Kahn A, et al. Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting frommultiple alternative first exons. FEBS. 1994;220:729.
38. Bulbarelli A, Valentini A, DeSilvestris M, et al. An erythroidspecific transcript generates the soluble form of NADHcytochrome b5 reductase in humans. Blood. 1998;92:310-319.
39. Borgese N, Pietrini G. Distribution of the integral membrane protein NADH-cytochrome b5 reductase in rat liver cells, studied with a quantitative radioimmunoblotting assay. Biochem J. 1986;239:393-403.
40. Tamura M, Yubisui T, Takeshita M, et al. Structural comparison of bovine erythrocyte, brain, and liver NADHcytochrome b5 reductase by HPLC mapping. J Biochem (Tokyo). 1987;101:1147-1159.
41. Ozols J, Korza G, Heinemann, FS, et al. Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase. J Biol Chem. 1985;260:11953-11961.
42. Yubisui T, Naitoh Y, Zenno S, et al. Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase. Proc Natl Acad Sci USA. 1987;84:3609-3613.
43. Zenno S, Hattori M, Misumi Y, et al. Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and the corresponding gene. J Biochem (Tokyo). 1990;107:810-816.
44. Hultquist D, Passon P. Catalysis of methemoglobin reduction by erythrocyte cytochrome b5 and cytochrome b5 reductase. Nature. 1971;229:252.
45. Kitajima S, Yasukochi Y, Minakami S. Purification and properties of human erythrocyte membrane NADH-cytochrome b5 reductase. Arch Biochem Biophys. 1981;210:330.
46. Dekker J, Eppink M, van Zwieten R, et al. Seven new nucleotides in the nicotinamide adenine dinucleotide reduced-cytochrome b(5) reductase gene leading to methemoglobinemia type I. Blood. 2001;97:1106-1114.
47. Gonzalez R, Estrada M, Wade M, et al. Heterogeneity of hereditary methaemoglobinaemia: a study of 4 Cuban families with NADH-Methaemoglobin reductase deficiency including a new variant (Santiago de Cuba variant). Scand J Haematol. 1978;20(5):385-393.
48. Board P, Petcock M. Methaemoglobinaemia resulting from heterozygosity for two NADH-methaemoglobin reductase variants: characterization as NADH-ferricyanide reductase. Br J Haematol. 1981;47:361-370.
49. Jaffe E. Hereditary methemoglobinemias associated with abnormalities in the metabolism of erythrocytes. Ann J Med. 1962;32:512.
50. Waller H. Inherited methemoglobinemia (enzyme deficiencies). Humangenetik. 1970;9:217.
51. Cohen R, Sachs J, Wicker D, et al. Methemoglobinemia provoked by malarial chemoprophylaxis in Vietnam. New Engl J Med. 1968;279:1127.
52. Scott E, Hoskins D. Hereditary methemoglobinemia in Alaskan Eskimos and Indians. Blood. 1958;13:795.
53. Scott E. The relation of diaphorase of human erythrocytes to inheritance of methemoglobinemia. J Clin Invest. 1960;39:1176.
54. Balsamo P, Hardy W, Scott E. Hereditary methemoglobinemia due to diaphorase deficiency inNavajo Indians. J Pediatr. 1964;65:928.
55. Ilinskaia I, Derviz G, Lavrova O, et al. Enzymatic methemoglobinemia. In: Papers of the Symposium: Biological Problems of the North State University, Yakutsk, and 1974: 226.
56. Andreeva A, Dmitrieva M, Levina A, et al. Molecular basis for disorders in the functional properties of hemoglobin in patients with enzymopenic methemoglobinemia. Papers of the 49th Scientific Session of the Central Scientific Research Institute of Hematology and Blood Transfusion. 1979;SSSR:73.
57. Prchal J, Borgese N, Moore M, et al. Congenital methemoglobinemia due to methemoglobin reductase deficiency in two unrelated American black families. Am J Med. 1990;89:516.
58. Katsube T, Sakamoto N, Kobayashi Y, et al. Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency. AmJ Hum Genet. 1991;48(4):799-808.
59. Shirabe K, Yubisui T, Borgese N, et al. Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem. 1992;267:20416-20421.
60. Leroux A, Junien C, Kaplan J-C, et al. Generalised deficiency of cytochrome b5 reductase in congenital methaemoglobinaemia with mental retardation. Nature. 1975;258:619.
61. Takeshita M, Tamura M, Kugi M, et al. Decrease of palmitoyl-CoA elongation in platelets and leukocytes in the patient of hereditary methemoglobinemia associated with mental retardation. Biochem Biophys Res Commun. 1987;148:384-391.
62. Kobayashi Y, Fukumaki Y, Yubisui T, et al. Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type. Blood. 1990;75:1408-1413.
63. Shirabe K, Fujimoto Y, Yubisui T, et al. An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOHterminal region of the enzyme. J Biol Chem. 1994;269:5952-5957.
64. Jenkins M, Prchal J. A novel mutation found in the NADHcytochrome b5 reductase gene in African-American family with type I congenital methemoglobinemia. Blood. 1995;86:649.
65. Shirabe K, Landi M, Takeshita M, et al. A novel point mutation in a 3ʹ splice site of the NADH-cytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia. AmJ Hum Genet. 1995;57:302-310.
66. Vieira L, Kaplan JC, Kahn A, et al. Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. Blood. 1995;85:2254-2262.
67. Manabe J, Arya R, Sumimoto H, et al. Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia. Blood. 1996;88:3208-3215.
68. Owen E, Berens J, Marinaki AM, et al. Recessive congenital methaemoglobinaemia type II a new mutation which causes incorrect splicing in the NADH-cytochrome b5 reductase gene. J InheritMetab Dis. 1997;20:610.
69. Hegesh E, Hegesh J, Kaftory A. Congenital methemoglobinemia with a deficiency of cytochrome b5. N Engl J Med. 1986;314:757.
70. Giordano S, Kaftory A, Steggles A. A splicing mutation in the cytochrome b5 gene from a patient with congenital methemoglobinemia and pseudohermaphrodism. Hum Genet. 1994;93:568.
71. Townes P, Morrison M. Investigation of the defect in a variant of hereditary methemoglobinemia. Blood. 1962;19:60.
72. Mansouri A, Lurie AA. Concise review: methemoglobinemia. Am J Hematol. 1993;42:7-12.
73. Coleman M, Coleman NA. Drug-induced methaemoglobinaemia. Treatment issues. Drug Saf. 1996;14:394-405.
74. Hadjiliadis D, Govert J.Methemoglobinemia after infusion of ifosfamide chemotherapy: first report of a potentially serious adverse reaction related to ifosfamide. Chest. 2000;118:1208.
75. Kizer N, Martinez E, Powell M. Report of two cases of rasburicase-induced methemoglobinemia. Leuk Lymphoma. 2006;47:2648-2650.
76. Daly J, Hultquist D, Rucknagel D. Phenazopyridine induced methaemoglobinaemia associated with decreased activity of erythrocyte cytochrome-b5 reductase. J Med Genet. 1983;20:307.
77. Linden C, Burns MJ. Poisoning and drug overdosage. In: Braunwald E FA, Kasper D, Hauser S, Longo D, Jameson J, et al., eds. Harrison's Principles of Internal Medicine 15th ed: New York:McGraw-Hill; 2001:2612.
78. Ash-Bernal R, Wise R, Wright SM. Acquired methemoglobinemia: a retrospective series of 138 cases at 2 teaching hospitals.Medicine (Baltimore). 2004;83:265.
79. Moore T, Walsh CS, Cohen MR. Reported adverse event cases of methemoglobinemia associated with benzocaine products. Arch InternMed. 2004;164:1192-1196.
80. Novaro G, Aronow H, Militello M, et al. Benzocaine-induced methemoglobinemia: experience from a high-volume transesophageal echocardiography laboratory. J Am Soc Echocardiogr. 2003;16:170.
81. Ross J. Deficient activity of DPNH-dependent methemoglobin diaphorase in cord blood erythrocytes. Blood. 1963; 21:51.
82. Bartos H, Desforges J. ErythrocyteDPNH-dependent diaphorase levels in infants. Pediatrics. 1966;37:991.
83. Eng L, Loo M, Fah FK. Diaphroase activity and variants in normal adults and newborns. Br J Haematol. 1972;23:419.
84. Comly H. Cyanosis in infants caused by nitrates in well water. JAMA. 1945;129:112.
85. Kross B, Ayebo A, Fuortes L.Methemoglobinemia: nitrate toxicity in rural America. AmFamPhysician. 1992;46:183.
86. Greer F, Shannon M. Infant methemoglobinemia: the role of dietary nitrate in food and water. Pediatrics. 2005;116:784-786.
87. Heyman I. Methemoglobinemia in infants. Harefuah. 1954; 46:144.
88. Yano S, Danish E, Hsia Y. Transient methemoglobinemia with acidosis in infants. J Pediatr. 1982;100:415.
89. Hegesh E, Shiloah, J. Blood nitrates and infantile methemoglobinemia. Clin Chim Acta. 1982;125:107.
90. Pollack E, Pollack CJ. Incidence of subclinical methemoglobinemia in infants with diarrhea. Ann Emerg Med. 1994;24:652.
91. Hanakoglu A, Danon P. Endogenous methemoglobinemia associated with diarrheal disease in infancy. J Pediatr Gastroenterol and Nutr. 1996;23:1.
92. Carlson G, Negri E, McGrew A, et al. Two cases of methemoglobinemia from the use of topical anesthetics. J Emerg Nurs. 2003;29:106-108.
93. Kilbourn R, Belloni P. Endothelial cell production of nitrogen oxides in response to interferon gamma in combination with tumor necrosis factor, interleukin-1, or endotoxin. J Natl Cancer Inst. 1990;82:772-776.
94. Moncada S, Palmer, RMJ, Higgs EA. Nitric oxide: Physiology, pathophysiology, and pharmacology. Pharmacol Rev. 1991;43:109-142.
95. Szabo C, Thiemermann C. Role of nitric oxide in haemorrhagic, traumatic and anaphylactic shock and in thermal injury. Shock. 1994;2:145-155.
96. Sharma V, Isaacson RA, John ME, et al. Reaction of nitric oxide with heme proteins: Studies on metmyoglobin, opossum methemoglobin and microperoxidase. Biochemistry. 1983;22:3897-3902.
97. Wennmalm A, Benthin G, Patersson AS. Dependence of the metabolism of nitric oxide in healthy human whole blood on the oxygenation of its red cell hemoglobin. Br J Pharmacol. 1992;106:507-508.
98. Chou T, Gibran NS, Urdahl K, et al.Methemoglobinemia secondary to topical silver nitrate therapy-a case report. Burns. 1999;25:549-552.
99. Bhattacharya J, Swarup-Mitra, S. Role of Plasmodium vivax in oxidation of haemoglobin in red cells of the host. Indian J Med Res. 1986;83:111-113.
100. Baird J, Lacy MD, Basri H, et al. Randomized, parallel placebo-controlled trial of primaquine for malaria prophylaxis in Papua, Indonesia. Clin Infect Dis. 2001;33:1990-1997.
101. Maran J, Guan Y, Ou CN, et al.Heterogeneity of the molecular biology of methemoglobinemia: a study of eight consecutive patients. Haematologica. 2005;90:687.
102. Barker S, Tremper K, Hyatt J. Effects of methemoglobinemia on pulse oximetry and mixed venous oximetry. Anesthesiology. 1989;70:112.
103. Kelner M, Bailey D. Mismeasurement of methemoglobin ("methemoglobin revisited"). Clin Chem. 1985;31:168.
104. Molthrop D, Wheeler, R, Hall K, et al. Evaluation of the methemoglobinemia associated with sulofenur. Invest New Drugs. 1994;12:99.
105. Evelyn K, Malloy H. Microdetermination of oxyhemoglobin, methemoglobin, and sulfhemoglobin in a single sample of blood. J Biol Chem. 1938;126:655.
106. Barker S, Curry J, Redford D, et al. Measurement of carboxyhemoglobin and methemoglobin by pulse oximetry: a human volunteer study. Anesthesiology. 2006;105:892-897.
107. Beutler E, Baluda M. Methemoglobin reduction: Studies of the interaction between cell populations and of the role of methylene blue. Blood. 1963;22:323.
108. Jaffe E. Hereditary methemoglobinemias associated with abnormalities in the metabolism of erythrocytes. Am J Med. 1966;41:786.
109. Jaffe E, Hsieh H. DPNH-methemoglobin reductase deficiency and hereditary methemoglobinemia. Semin Hemat. 1971;8:417.
110. Hegesh E, Calmanovici N, Avron M. New method for determining ferrihemoglobin reductase (NADH-methemoglobin reductase) in erythrocytes. J Lab ClinMed. 1968;72:339.
111. Board P. NADH-ferricyanide reductase, a convenient approach to the evaluation of NADH-methaemoglobin reductase in human erythrocytes. Clin Chim Acta. 1981;109: 233.
112. Kaftory A, Freundlich E, Manaster J, et al. Prenatal diagnosis of congenital methemoglobinemia with mental retardation. Isr J Med Sci. 1986;22:837.
113. Leroux A, Leturcq F, Deburgrave N, Szajnert MF. Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: novel mutation in the NADH-cytochrome b5 reductase gene leading to stop codon read-through. Eur J Haematol. 2005;74:389-395.
114. Arnold H, Botcher H, Hufnagel D, et al. Hereditary methemoglobinemia due to methemoglobin reductase deficiency in erythrocytes and leukocytes without neurological symptoms (abstract). In: XVII Congress of the International Society of Hematology. Paris; 1978:752.
115. Tanishima K, Tanimoto K, Tomoda A, et al.Hereditary methemoglobinemia due to cytochrome b5 reductase deficiency in blood cells without associated neurologic and mental disorders. Blood. 1985;66:1288.
116. Nagai T, Shirabe K, Yubisui T, et al. Analysis of mutant NADH-cytochrome b5 reductase: apparent "type III" methemoglobinemia can be explained as type I with an unstable reductase. Blood. 1993;81:808.
117. Beutler E.Methemoglobinemia and other causes of cyanosis. In: Beutler E, Lichtman MA, Coller B, Kipps, TJ, eds.Williams' Hematology. 5th ed. New York:McGraw-Hill; 1995:654.
118. Kaplan J, Chirouze M. Therapy of recessive congenital methaemoglobinemia by oral riboflavin. Lancet. 1978;2:1043.
119. Goluboff N, Wheaton, R. Methylene blue induced cyanosis and acute hemolytic anemia complicating the treatment of methemoglobinemia. J Pediatr. 1961;58:86.
120. Harvey J, Keitt A. Studies of the efficacy and potential hazards of methylene blue therapy in aniline-induced methemoglobinemia. Br J Haematol. 1983;54:29.
121. Rosen P, Johnson C, McGehee WG, et al. Failure of methylene blue treatment in toxic methemoglobinemia: associations with glucose-6-phosphate dehydrogenase deficiency. Ann InternMed. 1971;75:83.
122. Goldstein G, Doull J. Treatment of nitrite-induce methemoglobinemia with hyperbaric oxygen. Proc Soc Experimental Biology andMedicine. 1971;138:134.
123. Coleman M, Rhodes LE, Scott AK, et al. The use of cimetidine to reduce dapsone-dependent methaemoglobinaemia in dermatitis herpetiformis patients. Br J Clin Pharmacol. 1992;34:244.
124. Vreman H, Mahoney JJ, Stevenson DK. Carbon monoxide and carboxyhemoglobin. Adv Pediatr. 1995;42:303-325.
125. Hampson N. Trends in the incidence of carbon monoxide poisoning in theUnited States. AmJ EmergMed. 2005;23:838-841.
126. Hampson N. Emergency department visits for carbon monoxide poisoning in the Pacific northwest. J Emerg Med. 1998;16:695-698.
127. Weaver L. Carbon monoxide poisoning. Crit Care Clin. 1999;15:297-317.
128. Ernst A, Zibrak JD. Carbon monoxide poisoning. N Engl J Med. 1998;339:1603-1608.
129. Centres for Disease Control and Prevention C. Carbon monoxide poisoning from hurricane-associated use of portable generators-Florida 2004. MMWR. 2005;54:697-700.
130. Centers for Disease Control and Prevention C. Unintentional non-fire-related carbon monoxide exposures-United States, 2001-2003. MMWR. 2005;54:36-39.
131. Mott J, Wolfe MI, Alverson CJ, et al. National vehicle emissions policies and practices and declining US carbon monoxide-related mortality. JAMA. 2002;288:988-995.
132. Harper A, Croft-Baker J. Carbon monoxide poisoning: undetected by both patients and their doctors. Age Ageing. 2004;33:105-109.
133. US Environmental Protection Agency Emission facts: Idling vehicle emissions. US Environmental Protection Agency, Washington, DC; 1998 Publication EPA420-F-98-014 1998.
134. Centers for Disease Control and Prevention Carbon monoxide poisoning fromhurricane-associated use of portable generators-Florida 2004. MMWR. 2005;54:697-700.
135. Stewart R, Fisher TN, Hosko MJ, et al. Carboxyhemoglobin elevation after exposure to dichloromethane. Science. 1972;176:295-296.
136. Antonini E, Brunori M. Hemoglobin and myoglobin in their reactions with ligands. In: Neuberger A, Tatum EL, eds. Frontiers of Biology. Amsterdam, London: North-Holland Publishing Company; 1971.
137. Bunn H, Forget BG.Hemoglobin:Molecular, Genetic and Clinical Aspects. New York: Saunders; 1986.
138. Cheng X, Schoenborn BP. Neutron diffraction study of carbon-monoxymyoglobin. JMol Biol. 1991;220:381-399.
139. Kachalova G, Popov AN, Bartunik HD. A steric mechanism for inhibition of CO binding of heme proteins. Science. 1999;284:473-476.
140. Sjostrand T. Endogenous formation of carbon monoxide in man. Nature. 1949;164:580-581.
141. Coburn R, Danielson GK, Blakemore WS, et al. Carbon monoxide in blood: Analytical method and sources of error. J Appl Physiol. 1964;19:510-515.
142. Coburn R, Williams WJ, Kahn SB. Endogenous carbon dioxide production in patients with hemolytic anemia. J Clin Invest. 1966;44:460-468.
143. EPA. 600/8-90/045F: Air Quality Criteria for Carbon Monoxide. Research Triangle Park, NC, Environmental Criteria and Assessment Office, Office of Health and Environmental Assessment, Office of Research and Development, US Environmental Protection Agency, 1991:1-1 to 12-23.
144. Marks G, Brien JF, Nakatsu K, et al. Does carbon monoxide have a biological function? Trends Pharmacol Sci. 1991;12:185-188.
145. McGrath J. Effects of altitude on endogenous carboxyhemoglobin levels. J Toxicol Environ Health. 1992;35:127-33.
146. Giacometti G, Brunori, M, Antonini E, et al. The reaction of hemoglobin Zurich with oxygen and carbon monoxide. J Biol Chem. 1980;255:6160-6165.
147. Balster R, Ekelund LG, Grover RF. Evaluation of subpopulations potentially at risk to carbon monoxide exposure, in EPA 600/8-90/045F: Air quality criteria for carbon monoxide. Research Triangle Park, NC, Environmental Criteria and Assessment Office, Office of Health and Environmental Assessment, Office of Research and Development, US Environmental Protection Agency 1991:12-1 to 12-23.
148. Hampson N, Dunford RG, Kramer CC, et al. Selection criteria utilized for hyperbaric oxygen treatment of carbon monoxide poisoning. J EmergMed. 1995;13:227-231.
149. Benesch R, Maeda N, Benesch R. 2, 3-Diphosphoglycerate and the relative affinity of adult and fetal hemoglobin for oxygen and carbon dioxide. Biochim Biophys Acta. 1972;257:178-182.
150. Engel R, Rodkey FL, O'Neal JD, et al. Relative affinity of human fetal hemoglobin for CO and O2. Blood. 1969;33:37-45.
151. Gemelli F, Cattani R. Carbon monoxide poisoning in childhood. BrMed J. 1985;291:1197.
152. Lacey D. Neurologic sequellae of acute carbon monoxide intoxication. AmJ Dis Child. 1981;135:145-147.
153. Kao L, Nanagas KA. Carbon monoxide poisoning. EmergMed Clin North Am. 2004;22:985-1018.
154. Elkharrat D, Raphael JC, Korach JM, et al. Acute carbon monoxide intoxication and hyperbaric oxygen in pregnancy. Intensive CareMed. 1991;17:289-292.
155. Koren G, Sharav T, Pastuszak A, et al. A multicenter, prospective study of fetal outcome following accidental carbon monoxide poisoning in pregnancy. Reprod Toxicol. 1991;5:397-403.
156. Evans A, Enzer N, Eder HA, et al. Hemolytic anemia with paroxymal methemoglobnemia and sulfhemoglobinemia. Arch InternMed. 1950;86:22.
157. Bradenburg R, Smith HL. Sulfhemoglobinemia: a study of 62 clinical cases. Am Heart J. 1951;42:582.
158. Reynolds T, Ware AG. Sulfhemoglobinemia following habitual use of acetanilid. JAMA. 1952;149:538-542.
159. Cumming R, Pollock A. Drug induced sulphaemoglobinemia and Heinz body anemia in pregnancy with involvement of the foetus. ScottMed J. 1967;12:320-322.
160. Kneezel LD, Kitchens CS. Phenacetin-induced sulfhemoglobinemia: Report of a case and review of the literature. Johns HopkinsMed J. 1967;139:175-180.
161. Lambert M, Sonnet J, Mahien P, et al. Delayed sulfhemoglobinemia after acute dapsone intoxication. Clin Toxicol. 1982;19:45-49.
162. Ford R, Shkov J, Akman WV, et al. Deaths from asphyxia among fisherman. PFR: MMWR. 1978;27:309.
163. Madeiros M, Bechara EJ, Naoum PC, et al. Oxygen toxicity and hemoglobinemia in subjects from a highly polluted town. Arch Environ Health. 1983;38:11-15.
164. Carrico R, Blumberg WE, Peisach J J. The reversible binding of oxygen to sulfhemoglobin. J Biol Chem. 1978;253:7212-7215.
165. Park C, Nagel RL. Sulfhemoglobinemia. Clinical and molecular aspects.NEngl J Med. 1984;310:1579-1584.
166. Park C, Nagel RL, Blumberg WE. Sulfhemoglobin. Properties of partially sulfurated tetramers. J Bio Chem. 1986;261:8805-8810.
167. Berzofsky J, Peisach J, Blumberg WE. Sulfheme proteins. II. The reversible oxygenation of ferrous sulfmyoglobin. J Biol Chem. 1971;246:7366-7372.
168. Nichol A, Hendry I, Movell DB, et al. Mechanism of formation of sulfhemoglobin. Biochim Biophys Acta. 1968;156:97-103.
169. Kiese M. The biochemical production of ferrihemoglobinforming derivatives from aromatic amines and mechanisms of ferrihemoglobin formation. Pharmacol Rev. 1966;18:1091-1161.
170. McCutcheon A. Sulphaemoglobinaemia and glutathione. Lancet. 1960;2:290.
171. Gibson Q, Roughton, FJW. The kinetics and equilibria of the reactions of nitric oxide with sheep haemoglobin. J Physiol. 1957;136:507-526.
172. Suzuki T, Hayshi A, Shimizu A, et al. The oxygen equilibrium of hemoglobin M Saskatoon. Biochim. Biophys Acta. 1966;127:280-282.
173. Basch F. On hydrogen sulfide poisoning from external application of elementary sulfur as an ointment. Arch Exp Pathol Pharmacol. 1926;111:126.
174. Glud T. A case of enterogenic cyanosis? Complete recovery from acquired met-and sulfhemoglobinemia following treatment with neomycin and bacitracin. Ugeskr Laeg. 1979;141:1410-1411.
175. Burnett E, King EG, Grace M, et al. Hydrogen sulfide poisoning: review of 5 years' experience. Can Med Assoc. 1977;117:1277-1280.
176. Afane Ze E, Roche N, Atchou G, et al. Respiratory symptoms and peak expiratory flow in survivors of the Nyos disaster. Chest. 1996;110:1278-1281.
177. Ensabella F, Spirito A, Dupre S, et al.Measurement of sulfhemoglobin (S-Hb) blood levels to determine individual hydrogen sulfide exposure in thermal baths in Italy. Italian. Ig Sanita Pubbl. 2004;60:201-217.