PubMed · 3334511
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M Nagai. 1987. [Hemoglobin M].. https://pubmed.ncbi.nlm.nih.gov/3334511/
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The ferrous iron of hemoglobin is exposed continuously to high concentrations of oxygen and, thereby, is oxidized slowly to methemoglobin, a protein unable to carry oxygen. To restore hemoglobin function, methemoglobin (ferrihemoglobin) must be reduced to hemoglobin (ferrohemoglobin). Under physiological conditions, methemoglobin reduction is accomplished mainly by red cell NADH-cytochrome b5 reductase (NADH-methemoglobin reductase) so efficiently that there is insignificant amounts of methemoglobin in the circulating blood. However, should methemoglobin formation be increased--e.g., due to the presence of oxidant drugs, or an abnormal methemoglobin not amenable to reduction (hemoglobin M), or a deficiency in red cell cytochrome b5 reductase--methemoglobinemia will result. Most methemoglobinemias have no adverse clinical consequences and need not be treated. Under certain conditions, such as exposure to large amounts of oxidant or in young infants, rapid treatment is necessary. In hereditary cytochrome b5 deficiency, treatment is often directed at improving the poor cosmetic effect of persistent cyanosis with the minimum amount of drugs to give satisfactory clinical results.
The characterization of two human haemoglobin variants, Hb M Hyde Park and Hb San José, by fast atom bombardment mass spectrometry is reported. The identification of the site and nature of the amino acid substitution was performed by analysis of the peptide mixture generated by proteolytic digestion of the variant beta-globin chains with V-8 protease. The use of this protease was instrumental in the unambiguous identification of the replaced residues because the tryptic map alone was unable to unequivocally locate the modification. Spectra obtained were easily interpreted and the characterization of Hb M Hyde Park (beta, 92 Hys leads to Tyr) and Hb San José (beta 7 Glu leads to Gly) was accomplished essentially by the same procedure already described for the tryptic map. These results are suggestive of alternative approaches in haemoglobin variants characterization using different proteolytic enzymes when tryptic data alone do not lead to unambiguous results.