Heme in the treatment of heme deficiency states

References

• Kappas A., Sassa A., Anderson K. E. The Porphyrias. Metabolic Basis of Inherited Diseases, J. B. Stanbury, J. B. Wyngaarden, D. ES Fredrickson. McGraw-Hill, New York 1983; 1301–84
   Google Scholar
• Bonkowsky H. L., Tschudy D. P., Collins A., Doherty J., Bossenmaier I., Cardinal R., Watson C. J. Repression of porphyrin precursors in acute intermittent porphyria by intravenous infusions of hematin. Proc Natl Acad Sci 1971; 68: 2725–9
   PubMed Web of Science ®Google Scholar
• Tschudy D. P., Lamon J. P. Porphyrin metabolism and the porphyrias. Metabolic Control and Disease, P. K. Bondy, L. E. Rosenberg. Saunders, Philadelphia 1980; 939–1007
   Google Scholar
• May K. M., Bawden M. J. Control of heme biosynthesis in animals. Semin Hematol 1989; 26: 150–6
   PubMed Web of Science ®Google Scholar
• Sassa S. Heme stimulation of cellular growth and differentiation. Semin Hematol 1988; 25: 312–20
   PubMed Web of Science ®Google Scholar
• Muller-Eberhard U., Nikkilä H. Transport of tetrapyrroles by proteins. Semin Hematol 1989; 24: 86–104
   Google Scholar
• Muller-Eberhard U., Vincent S. H. Commentary. Concepts of heme distribution within hepatocytes. Biochem Pharmacol 1985; 34: 719–25
   PubMed Web of Science ®Google Scholar
• Whiting M. J., Granick S. δ-Aminolevulinic acid synthase from chick embryo liver mitochondria. I. Purification and some properties. J Biol Chem 1976; 251: 1340–7
   PubMed Web of Science ®Google Scholar
• Aoki Y., Wada O., Urata G., Takaku F., Nakao K. Purification and some properties of δ-aminolevulinate (ALA) synthetase in rabbit reticulocytes. Biochem Biophys Res Commun 1971; 42: 568–75
   PubMed Web of Science ®Google Scholar
• Granick S., Sinclair P., Sassa S., Grieninger G. Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and spectrofluorometric assay for porphyrin composition. J Biol Chem 1975; 250: 9215–25
   PubMed Web of Science ®Google Scholar
• Srivastava G., Brooker J. D., May B. K., Elliot W. H. Haem control in experimental porphyria. The effect of haemin on the induction of δ-aminolaevulinate synthase in isolated chick-embryo liver cells. Biochem J 1980; 188: 781–8
   PubMed Web of Science ®Google Scholar
• Wolfson S. J., Bartczak A., Bloomer J. R. Effect of endogenous heme generation on δ-aminolevulinic acid synthase activity in rat liver mitochondria. J Biol Chem 1979; 254: 3543–6
   PubMed Web of Science ®Google Scholar
• Giger U., Meyer U. A. Role of haem in the induction of cytochrome P-450 by phenobarbitone. Biochem J 1981; 198: 321–9
   PubMed Web of Science ®Google Scholar
• Bottomley S. S., Muller-Eberhard U. Pathophysiology of heme synthesis. Semin Hematol 1988; 25: 282–302
   PubMed Web of Science ®Google Scholar
• Ortiz de Montellano P. R., Correia M. A. Suicidal destruction of cytochrome P-450 during oxidative drug metabolism. Ann Rev Pharmacol Toxicol 1983; 23: 481–503
   PubMed Web of Science ®Google Scholar
• Bawden M. J., Borthwick I. A., Healy H. M., Morris C. P., May B. K., Elliott W. H. Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res 1987; 15: 8563
   PubMed Web of Science ®Google Scholar
• Borthwick I. A., Srivastava G., Day A. R., Pirola B. A., Snoswell M. A., May B. K., Elliott W. H. Complete nucleotide sequence of hepatic 5-aminolevulinate synthase precursor. Eur J Biochem 1985; 150: 481–4
   PubMedGoogle Scholar
• Srivastava G., Borthwick I. A., Maguire D. J., Elferink C. J., Bawden M. J., Mercer J. FB, May B. K. Regulation of 5-aminolevulinate synthase mRNA in different rat tissues. J Biol Chem 1988; 263: 5202–9
   PubMed Web of Science ®Google Scholar
• Hamilton J. W., Bement W. J., Sinclair P. R., Sinclair J. F., Wetterhahn K. E. Expression of 5-aminolevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Biochem J 1988; 255: 267–75
   PubMed Web of Science ®Google Scholar
• Tschudy D. P., Hess R. A., Frykholm B. C. Inhibition of δ-aminolevulinic acid dehydratase by 4,6-dioxoheptanoic acid. J Biol Chem 1981; 256: 9915–23
   PubMed Web of Science ®Google Scholar
• Hayashi N., Kuroshima Y., Kikuchi G. Mechanism of allylisopropylacetamide-induced increase of δ-aminolevulinate synthetase in rat liver mitochondria. Arch Biochem Biophys 1972; 148: 10–21
   PubMed Web of Science ®Google Scholar
• Ibraham N. G., Friedland M. L., Levere R. D. Heme metabolism in erythroid and hepatic cells. Progress in Hematology, E. B. Brown. Grune & Stratum, Philadelphia 1983; 75–130
   Google Scholar
• Pain V. M. Initiation of protein synthesis in mammalian cells. Biochem J 1986; 235: 625–37
   PubMed Web of Science ®Google Scholar
• Ponka P., Schulman H. M. Acquisition of iron from transferrin regulates reticulocyte heme synthesis. J Biol Chem 1985; 260: 14717–21
   PubMed Web of Science ®Google Scholar
• Ponka P., Schulman H. M., Martinez-Medellin J. Haem inhibits iron uptake subsequent to endocytosis of transferrin in reticulocytes. Biochem J 1988; 251: 105–9
   PubMed Web of Science ®Google Scholar
• Gardner L. C., Cox T. M. Biosynthesis of heme in immature erythroid cells. J Biol Chem 1988; 263: 6676–82
   PubMed Web of Science ®Google Scholar
• Elferink C. J., Sassa S., May B. K. Regulation of 5-aminolevulinate synthase in mouse erythroleukemic cells is different from that in liver. J Biol Chem 1988; 263: 13012–6
   PubMed Web of Science ®Google Scholar
• Riddle R. D., Yamamoto M., Engel J. O. Expression of δ-aminolevulinate synthase in avian cells: Separate genes encode erythroid-specific and non-specific isozymes. Proc Natl Acad Sci USA 1989; 86: 792–6
   PubMed Web of Science ®Google Scholar
• Brown S. B., Shillcock M., Jones P. Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution. Biochem J 1976; 153: 279–85
   PubMed Web of Science ®Google Scholar
• Heaven G. H., Chen S-H, d'Albis A., Gratzer W. B. A spectrophotometric study of the haemin-humanserum-albumin system. Eur J Biochem 1974; 41: 539–46
   PubMedGoogle Scholar
• Liem H. H., Muller-Eberhard U. Do heme and bilirubin have identical binding sites on the albumin molecule?. Biochem Biophys Res Commun 1971; 42: 634–9
   PubMed Web of Science ®Google Scholar
• Bratlid D. Reserve albumin binding capacity, salicylate saturation index, and red cell binding of bilirubin in neonatal jaundice. Arch Dis Child 1973; 48: 393–7
   PubMed Web of Science ®Google Scholar
• Brodersen R. Binding of bilirubin diaresis and other ligands to human serum albumin. Albumin: Structure, Biosynthesis, Function, T. Peters, I. Sjöholm. Pergamon, Oxford 1978; 61–8
   Google Scholar
• Brodersen R. Aqueous solubility albumin binding, and tissue distribution of bilirubin. Bile Pigments and Jaundice, J. D. Ostrow. Dekker, New York 1986; 157
   Google Scholar
• Hunt R., Cohen E., Smith A. Hemopexin and transferrin represent a specific class of receptor-mediated endocytotic transport systems. FASEB J 1988; 2: A574
   Web of Science ®Google Scholar
• Smith A., Morgan W. T. Haem transport to the liver by hemopexin: Receptor-mediated uptake with recycling of the protein. Biochem J 1979; 182: 47–54
   PubMed Web of Science ®Google Scholar
• Smith A., Morgan W. T. Hemopexin-mediated heme uptake by the liver: Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes. J Biol Chem 1984; 259: 12049–53
   PubMed Web of Science ®Google Scholar
• Majuri R., Gräsbeck R. Isolation of the haemopexin-haem receptor from pig liver cells. FEBS Lett 1986; 199: 80–4
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Gräsbeck R., Kouvonen I., Lundberg M. An intestinal receptor for heme: Its partial characterization. Int J Biochem 1980; 12: 713–6
   PubMedGoogle Scholar
• Taketani S., Kohno H., Naitoh Y., Tokunaga R. Isolation of the hemopexin receptor from human placenta. J Biol Chem 1987; 262: 8668–71
   PubMed Web of Science ®Google Scholar
• Alam J., Smith A. Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells. J Biol Chem 1989; 264: 17637–40
   PubMed Web of Science ®Google Scholar
• Reed R. G., Burrington C. M., Muller-Eberhard U. Differences in binding characteristics of serum albumin and hemopexin at hepatocyte surfaces. J Biol Chem 1988; 107: 146A
   Google Scholar
• Morgan W. T., Liem H. H., Sutor R. P., Muller-Eberhard U. Transfer of heme from heme-albumin to hemopexin. Biochim Biophys Acta 1976; 444: 435–45
   PubMed Web of Science ®Google Scholar
• Lane R. S., Rangeley D. M., Liem H. H., Wormsley S., Muller-Eberhard U. Plasma clearance of 1251-labelled haemopexin in normal and haem-loaded rabbits. Br J Haematol 1973; 25: 533–40
   PubMed Web of Science ®Google Scholar
• Eaton J. W., Brandt P., Mahoney J. R., Lee J. T. Haptoglobin: A natural bacteriostat. Science 1982; 215: 691–3
   PubMed Web of Science ®Google Scholar
• Gutteridge J. MC, Smith A. Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem J 1988; 256: 861–5
   PubMed Web of Science ®Google Scholar
• Zizkovsky V., Havranova M., Storp P., et al. A spectroscopic study of the hemin-human-alpha-fetoprotein system. Ann NY Acad Sci 1983; 417: 57–60
   PubMed Web of Science ®Google Scholar
• Poh-Fitzpatrick M. B., Zaider E., Lasker M. Erythropoietic protoporphyria vs. porphyria cutanea tarda: Different partitioning of porphyrins among gelfractioned serum proteins. Clin Res 1988; 36: 686A
   Google Scholar
• Morgan W. T., Koskelo P., Koenig H., et al. Human histidine-rich glycoprotein. II. Serum levels in adults, pregnant women, and neonates. Proc Soc Exp Bio Med 1978; 158: 647–51
   PubMed Web of Science ®Google Scholar
• Levi A. J., Gatmaitan C., Arias I. M. Two hepatic cytoplasmic protein fractions, Y and Z, and their possible role in the uptake of bilirubin, sulfobromophthalein, and other anions. J Clin Invest 1969; 48: 2156–67
   PubMed Web of Science ®Google Scholar
• Vincent S. H., Muller-Eberhard U. A protein of the Z class liver cytosolic proteins in the rat that prefentially binds heme. J Biol Chem 1985; 260: 14521–8
   PubMed Web of Science ®Google Scholar
• Hayes J. D., Mantle T. J. Use of immuno-blot techniques to discriminate between the glutathione S-transferase Yf, Yk, Ya, Yn/Yb, and Yc subunits and to study their distribution in extrahepatic tissues: Evidence for three immunochemically distinct groups of transferase in the rat. Biochem J 1986; 233: 779–88
   PubMed Web of Science ®Google Scholar
• Ketterer B., Beale D., Meyer D. The structure and multiple functions of glutathione transferases. Biochem Soc Trans 1982; 10: 82–4
   PubMed Web of Science ®Google Scholar
• Bhargava M. M., Listowsky I., Arias I. M. Ligandin: Bilirubin binding and glutathione-S-transferase activity are independent processes. J Biol Chem 1978; 253: 4112–5
   PubMed Web of Science ®Google Scholar
• Versee V., Barel A. O. Interactions of rat alpha-foetoprotein with bilirubin. Biochem J 1979; 179: 705–7
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Marver H. S., Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc Natl Acad Sci USA 1968; 61: 748–55
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Marver H. S., Schmid R. Microsomal heme oxygenase, Characterization of the enzyme. J Biol Chem 1969; 244: 6388–94
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Ross M. E., Marver H. S., Schmid R. Reduced nicotinamide adenine dinucleotide phosphate-dependent biliverdin reductase: Partial purification and characterization of the enzyme. Biochemistry 1970; 9: 293–303
   Web of Science ®Google Scholar
• Correia M. A., Farrell G. C., Schmid R., Ortiz de Montellano P. R., Yost G. S., Mico B. A. Incorporation of exogenous heme into hepatic cytochrome P-450 in vivo. J Biol Chem 1979; 254: 15–7
   PubMed Web of Science ®Google Scholar
• Badaway A. A-B, Evans M. The regulation of rat liver tryptophan pyrrolase by its cofactor haem. Experiments with hematin and 5-aminolaevulinate and comparison with the substrate and hormonal mechanisms. Biochem J 1975; 150: 511–20
   PubMed Web of Science ®Google Scholar
• Bissell D. M., Liem H. H., Muller-Eberhard U. Secretion of haem by hepatic parenchymal cells. Biochem J 1979; 184: 689–94
   PubMed Web of Science ®Google Scholar
• McCormack L. R., Liem H. H., Strum W. P. Grundy SM, Muller-Eberhard U. Effects of haem infusion on biliary secretion of porphyrins, haem, and bilirubin in man. Eur J Clin Invest 1982; 12: 257–62
   PubMed Web of Science ®Google Scholar
• Linden I-B, Tokola O., Karlsson M., Tenhunen R. Fate of haem after parenteral administration of haem arginate to rabbits. J Pharm Pharmacol 1987; 39: 96–102
   PubMed Web of Science ®Google Scholar
• Tokola O., Tenhunen R., Volin L., Mustajoki P. Pharmakokinetics of intravenously administered haem arginate. Br J Clin Pharmac 1986; 22: 331–5
   PubMed Web of Science ®Google Scholar
• Bonkowsky H. L., Tschudy D. P., Collins A., Doherty J., Bossenmaier I., Cardinal R., Watson C. J. Repression of the overproduction of porphyrin precursors in acute intermittent porphyria by intravenous infusions of hematin. Proc Natl Acad Sci USA 1971; 68: 2725–9
   PubMed Web of Science ®Google Scholar
• Watson C. J., Dhar J. G., Bossenmaier I., Cardinal I., Petryka Z. J. Effect of hematin in acute porphyric relapse. Ann Intern Med 1973; 79: 80–3
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Tokola O., Linden I-B. Haem arginate: A new stable haem compound. J Pharm Pharmacol 1987; 39: 780–6
   PubMed Web of Science ®Google Scholar
• Fuchs Th, Ippen H. Bahandlung der akut intermittierenden Porphyrie mil einem neuen, an Albumin gebundenen lyopholisierten Hämatin. Dtsch Med Wochenschr 1987; 112: 1302–5
   PubMed Web of Science ®Google Scholar
• Mustajoki P., Tenhunen R., Pierach C., Volin L. Heme in the treatment of porphyrias and hematological disorders. Semin Hematol 1989; 26: 1–9
   PubMed Web of Science ®Google Scholar
• Mustajoki P., Tenhunen R., Tokola O., Gothoni G. Haem arginate in the treatment of acute hepatic porphyrias. Br Med J 1986; 293: 538–9
   PubMed Web of Science ®Google Scholar
• Sievers G., Häkli H., Luhtala J., Tenhunen R. Optical and EPR spectroscopy studies on haem arginate, a new compound used for treatment of porphyria. Chem Biol Interactions 1987; 63: 105–14
   PubMed Web of Science ®Google Scholar
• Tokola O., Linden I-B, Tenhunen R. The effects of haem arginate and haematin upon allylisopropylacetamide induced experimental porphyria in rats. Pharmacol Toxicol 1987; 61: 75–8
   PubMedGoogle Scholar
• Herrick A., McLellan A., Brodie M. J., McColl K. EL, Moore M. R., Goldberg A. Effect of haem arginate therapy on porphyrin metabolism and mixed function oxygenase activity in acute hepatic porphyria. Lancet 1987; ii: 1178–9
   Google Scholar
• Pierach C. Hematin therapy for the porphyric attack. Semin Liver Dis 1982; 2: 125–31
   PubMedGoogle Scholar
• Watson C. J., Bossenmaier I., Cardinal R., Petryka Z. J. Repression by hematin of porphyrin biosynthesis in erythrocyte precursors in congenital erythropoietic porphyria. Proc Natl Acad Sci USA 1974; 71: 278–82
   PubMed Web of Science ®Google Scholar
• Bloomer J. R., Pierach C. A. Effect of hematin administration to patients with protoporphyria and liver disease. Hepatology 1982; 2: 817–21
   PubMed Web of Science ®Google Scholar
• Lamon J. L., Frykholm B. C., Hess R. A., Tschudy D. B. Haematin therapy for acute porphyria. Medicine 1979; 58: 252–69
   PubMed Web of Science ®Google Scholar
• Lamon J. L., Poh-Fitzpatrick M. B., Lamola A. A. Hepatic protoporphyrin production in human protoporphyria. Gastroenterology 1980; 79: 115–25
   PubMed Web of Science ®Google Scholar
• Anderson K. E., Alvares A. P., Sassa S., Kappas A. Studies in porphyria. Drug oxidation rates in hereditary hepatic porphyria. Clin Pharmacol Ther 1976; 19: 47–54
   PubMed Web of Science ®Google Scholar
• Birnie G. G., McColl K. EL, Thomson G. G., Moore M. R., Goldberg A., Brodie M. J. Antipyrine metabolism in acute hepatic porphyria in relapse and remission. Br J Pharmacol 1987; 23: 358–61
   Web of Science ®Google Scholar
• Tokola O., Mustajoki P., Himberg J-J. Haem arginate improves hepatic oxidative metabolism in variegate porphyria. Br J Pharmacol 1988; 26: 753–7
   Web of Science ®Google Scholar
• Ged C., Rouillon J. M., Pichard L., Combalbert J., Bressot N., Bories P., Michel H., Beaune P., Maurel P. The increase in urinary excretion of 6β-hydroxycortisol as amarker of human hepatic cytochrome P450IIIA induction. Br J Clin Pharmac 1989; 28: 373–87
   PubMed Web of Science ®Google Scholar
• Muller-Eberhard U., Eiseman J. L., Foidart M., Alvares A. P. Effect of heme on allylisopropylacetamide-induced changes in heme and drug metabolism in the rhesus monkey (Macaca Mulatta). Biochem Pharmacol 1983; 32: 3765–9
   PubMed Web of Science ®Google Scholar
• Lascelles J. The synthesis of enzymes concerned in bacteriochlorophyll foramtion in growing cultures of Rhodopseudomonas spheroides. J Gen Microbiol 1960; 23: 487–98
   PubMedGoogle Scholar
• Marver H. S., Tschudy D. P., Perlroth M. G., Collins A. Coordinate synthesis of heme and apoenzyme in the formation of tryptophan pyrrolase. Science 1966; 154: 501–3
   PubMed Web of Science ®Google Scholar
• Waxman A. D., Collins A., Tshudy D. P. Oscillations of hepatic δ-aminolevulinic acid synthetase produced in vivo by heme. Biochim Biophys Res Commun 1966; 24: 675–83
   PubMed Web of Science ®Google Scholar
• Watson C. J., Pierach C. A., Bossenmaier I., Cardinal R. Use of hematin in the acute attack of the “inducible” hepatic porphyrias. Adv Intern Med 1978; 23: 265–86
   PubMedGoogle Scholar
• McColl K. EL, Moore M. R., Thompson G. G., Goldberg A. Treatment with haematin in acute hepatic porphyria. C J Med 1981; 198: 161–74
   Google Scholar
• Herrick A. L., McColl K. EL, Moore M. R., Cook A., Goldberg A. Controlled trial of haem arginate in acute hepatic porphyria. Lancet 1989; i: 1295–7
   Google Scholar
• Bissell D. M. Treatment of acute hepatic porphyria with hematin. J Hepatol 1988; 6: 1–7
   PubMed Web of Science ®Google Scholar
• Goetsch C. A., Bissell D. M. Instability of hematin used in the treatment of acute hepatic porphyria. N Engl J Med 1986; 315: 235–8
   PubMed Web of Science ®Google Scholar
• Ruutu T., Volin L., Tenhunen R. Haem arginate as a treatment for myelodysplastic syndromes. Br J Haematol 1987; 65: 425–8
   PubMed Web of Science ®Google Scholar
• Volin L., Ruutu T., Knuutila S., Tenhunen R. Heme arginate treatment for myelodysplastic syndromes. Leuk Res 1988; 12: 423–31
   PubMed Web of Science ®Google Scholar
• Dhar G. J., Bossenmaier I., Cardinal R., Petryka Z. J., Watson C. J. Transitory renal failure following rapid administration of a relatively large amount of hematin in a patient with acute intermittent porphyria in clinical remission. Acta Med Scand 1978; 203: 437–43
   PubMedGoogle Scholar
• Glueck R., Green D., Cohen I., Ts'ao C. Hematin: Unique effects on hemostasis. Blood 1983; 61: 243–9
   PubMed Web of Science ®Google Scholar
• Morris D. L., Dudley M. D., Pearson R. D. Coagulopathy associated with hematin treatment for acute intermitteny porphyria. Ann Intern Med 1981; 95: 700–1
   PubMed Web of Science ®Google Scholar
• Petersen J. M., Pierach C. A. Hematin-induced hemolysis in acute porphyria. Ann Intern Med 1984; 101: 877–8
   PubMed Web of Science ®Google Scholar
• Neely S. M., Gardner D. V., Green D., Ts'ao C. Effect of hematin on endothelial cells and endolhelial cell-platelet interactions. Am J Pathol 1984; 115: 390–6
   PubMed Web of Science ®Google Scholar
• Volin L., Rasi V., Vahtera E., Tenhunen R. Heme arginate: Effects on Hemostasis. Blood 1988; 71: 625–8
   PubMed Web of Science ®Google Scholar
• Monette R. F., Murray J. C., Gelinas R., et al. Restriction endonuclease mapping of globin genomic regions of HEL (human erythroleukemia) line. Hemoglobin 1983; 7: 245–56
   PubMed Web of Science ®Google Scholar
• Porte P. N., Meints R. H., Mesner K. Enhancement of erythroid colony growth in culture by hemin. Exp Hematol 1979; 7: 11–6
   Web of Science ®Google Scholar
• Rutherford T. R., Clegg J. B., Weatherall D. J. K 562 human leukemic cells synthesize embryonic haemoglobin in responseto haemin. Nature 1979; 280: 164–5
   PubMed Web of Science ®Google Scholar
• Monette R. F., Holden S. A., Sheehy M. J., Matzinger E. A. Specificity of hemin action in vivo at early stages of hematopoietic cell differentiation. Exp Hematol 1984; 12: 782–7
   PubMed Web of Science ®Google Scholar
• Partanen S., Pasanen A., Juvonen E., Tenhunen R., Ruutu T. Erythroid colony formation and effect of hematin in vitro in hereditary sideroblastic anemias. Exp Hematol 1988; 16: 313–5
   PubMed Web of Science ®Google Scholar
• Volin L. Haem arginate treatment for hereditary sideroblastic anemia. Eur J Haematol 1989; 42: 60–6
   PubMed Web of Science ®Google Scholar
• Tischler P. V., Woodward B., O'Connor J., Holbrook D. A., Seidman L. J., Hallett M., Knighton D. J. High prevalence of intermittent acute porphyria in a psychiatric patient population. Am J Psychiatry 1985; 142: 1430–6
   PubMed Web of Science ®Google Scholar
• Lutton J. D., Abraham N. G., Friedland M., Levere R. D. The toxic effect of heavy metals on rat bone marrow erythropoiesis in vitro: Protective role of hemin and zinc. Environ Res 1984; 35: 97–103
   PubMed Web of Science ®Google Scholar
• Kay F. J., Weinberg R. S., Schofield J. M., Alter B. Hemin in sickle cell anemia. Int J Cell Cloning 1986; 4: 432–46
   Google Scholar
• Abraham N. G., Bucher D., Niranjan U., Brown A. C., Lutton J. D., Distenfeld A., Ahmed T., Levere R. D. Microenvironmental toxicity of azidothymidine: Partia sparing with hemin. Blood 1989; 74: 139–44
   PubMed Web of Science ®Google Scholar
• Tenhunen R., Savolainen H., Jäppinen P. Changes in haem synthesis associated with occupational exposure to organic and inorganic sulphides. Clin Sci 1983; 64: 187–91
   Web of Science ®Google Scholar
• Savolainen H., Jäppinen P., Tenhunen R. Reversal of sulfide-induced effects on porphyrin metabolism by exogenous heme. Res Commun Chem Pathol Pharmacol 1985; 50: 245–50
   PubMedGoogle Scholar