Table of Contents
ISRN Hematology
Volume 2011 (2011), Article ID 735314, 10 pages
http://dx.doi.org/10.5402/2011/735314
Research Article

Structural and Functional Characterization of a New Double Variant Haemoglobin (HbG-Philadelphia/Duarte 𝛼 𝟔 𝟖 A s n L y s 𝟐 𝛽 𝟔 𝟐 A l a P r o 𝟐 )

1Department of Sciences Applied to Biosystems, University of Cagliari, S.P. Monserrato-Sestu km 0.700, 09042 Monserrato, Italy
2Department of Chemical Sciences, University of Cagliari, S.P. Monserrato-Sestu km 0.700, 09042 Monserrato, Italy
3SLACS, Istituto Officina dei Materiali del CNR and Department of Physics, University of Cagliari, S.P. Monserrato-Sestu km 0.700, 09042 Monserrato, Italy
4Department of Biomedical and Biotecnologies Sciences, University of Cagliari, via Jenner, 09121 Cagliari, Italy

Received 8 September 2010; Accepted 4 October 2010

Academic Editors: J. S. Gibson, T. Ikuta, and D. Lavelle

Copyright © 2011 Antonella Fais et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. Giardine, S. van Baal, P. Kaimakis et al., “HbVar database of human hemoglobin variants and thalassemia mutations: 2007 update,” Human Mutation, vol. 28, no. 2, p. 206, 2007. View at Google Scholar · View at Scopus
  2. S. Fucharoen, Y. Changtrakun, T. Ratanasiri, G. Fucharoen, and K. Sanchaisuriya, “Complex interaction of Hb Hekinan [α27(B8) GluAsp] and Hb E [β26(B8) GluLys] with a deletional α-thalassemia 1 in a Thai family,” European Journal of Haematology, vol. 70, no. 5, pp. 304–309, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. K. Sanchaisuriya, S. Chunpanich, S. Fucharoen, G. Fucharoen, P. Sanchaisuriya, and Y. Changtrakun, “Association of Hb Q-Thailand with homozygous Hb E and heterozygous Hb Constant Spring in pregnancy,” European Journal of Haematology, vol. 74, no. 3, pp. 221–227, 2005. View at Publisher · View at Google Scholar · View at Scopus
  4. H. Wajcman and J. Riou, “Globin chain analysis: an important tool in phenotype study of hemoglobin disorders,” Clinical Biochemistry, vol. 42, no. 18, pp. 1802–1806, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. B. J. Wild and B. J. Bain, “Detection and quantitation of normal and variant haemoglobins: an analytical review,” Annals of Clinical Biochemistry, vol. 41, no. 5, pp. 355–369, 2004. View at Publisher · View at Google Scholar · View at Scopus
  6. H. Wajcman, J. Traeger-Synodinos, I. Papassotiriou et al., “Unstable and thalassemic α chain hemoglobin variants: a cause of Hb H disease and thalassemia intermedia,” Hemoglobin, vol. 32, no. 4, pp. 327–349, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. K. Adachi, S. Surrey, H. Tamary et al., “Hb Shelby [β131(H9)Gln→Lys] in association with Hb S [β6(A3)Glu→Val]: characterization, stability, and effects on Hb S polymerization,” Hemoglobin, vol. 17, no. 4, pp. 329–343, 1993. View at Google Scholar · View at Scopus
  8. T. H. J. Huisman, “Combinations of β chain abnormal hemoglobins with each other or with β-thalassemia determinants with known mutations: influence on phenotype,” Clinical Chemistry, vol. 43, no. 10, pp. 1850–1856, 1997. View at Google Scholar · View at Scopus
  9. E. Beutler, A. Lang, and H. Lehmann, “Hemoglobin Duarte: (α2β2 62(E6)Ala→Pro): a new unstable hemoglobin with increased oxygen affinity,” Blood, vol. 43, no. 4, pp. 527–535, 1974. View at Google Scholar · View at Scopus
  10. C. Baglioni and V. M. Ingram, “Abnormal human haemoglobins V. Chemical investigation of haemoglobins A, G, C, X from one individual,” Biochimica et Biophysica Acta, vol. 48, no. 2, pp. 253–265, 1961. View at Google Scholar · View at Scopus
  11. M. Ceccarelli, P. Ruggerone, R. Anedda et al., “Structure-function relationship in a variant hemoglobin: a combined computational-experimental approach,” Biophysical Journal, vol. 91, no. 9, pp. 3529–3541, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Takaoki, I. Iwao, Y. Kiyomi, O. Yuzo, and S. Susumu, “Amino acid substitution of hemoglobin ube 2 (α268aspβ2): an example of successful application of partial hydrolysis of peptide with 5% acetic acid,” Clinica Chimica Acta, vol. 16, no. 3, pp. 347–352, 1967. View at Google Scholar · View at Scopus
  13. I. Iuchi, S. Shimasaki, K. Hidaka, S. Ueda, and S. Shibata, “Hb Ube-2 (α68[E-17]Asn→Asp): the second instance in Japan,” Hemoglobin, vol. 5, no. 6, pp. 599–603, 1981. View at Google Scholar · View at Scopus
  14. M. L. North, M. C. Garel, J. Thillet, A. Gardea, J. M. Levy, and J. Rosa, “Clinica, structural and functional studies of Hb G-Philadelphia detected in a Maroccan newborn,” Nouvelle Revue Francaise d'Hematologie, vol. 18, no. 3, pp. 601–610, 1977. View at Google Scholar
  15. J. A. Pardoll, S. Charache, B. L. Hjelle et al., “Homozygous a thalassemia/HbG-philadelphia,” Hemoglobin, vol. 6, pp. 503–515, 1982. View at Google Scholar
  16. R. K. Saiki, D. H. Gelfand, S. Stoffel et al., “Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase,” Science, vol. 239, no. 4839, pp. 487–491, 1988. View at Google Scholar · View at Scopus
  17. B. Masala and L. Manca, “Detection of the common Hb F Sardinia [(A)γ(E19)Ile → Thr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes,” Clinica Chimica Acta, vol. 198, no. 3, pp. 195–202, 1991. View at Publisher · View at Google Scholar · View at Scopus
  18. G. D. Efremov, B. Markovska, N. Stojanovski, G. Petkov, N. Nikolov, and T. H. J. Huisman, “The use of globin chain electrophoresis in polyacrylamide gels for the quantitation of the γG to γA ratio in fetal hemoglobin,” Hemoglobin, vol. 5, no. 7-8, pp. 637–651, 1981. View at Google Scholar
  19. L. Manca, M. Formato, P. Demuro, D. Gallisai, M. Orzalesi, and B. Masala, “The gamma globin chain heterogeneity of the Sardinian newborn baby,” Hemoglobin, vol. 10, no. 5, pp. 519–528, 1986. View at Google Scholar
  20. M. Braend, L. L. Nesse, and G. D. Efremov, “Expression and genetics of caprine haemoglobins,” Animal Genetics, vol. 18, no. 3, pp. 223–231, 1987. View at Google Scholar · View at Scopus
  21. B. Giardina and G. Amiconi, “Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures,” Methods in Enzymology, vol. 76, pp. 417–427, 1981. View at Google Scholar · View at Scopus
  22. K. Imai, Allosteric Effects in Haemoglobin, Cambridge University Press, Cambridge, Mass, USA, 1982.
  23. G. Fermi, M. F. Perutz, B. Shaanan, and R. Fourme, “The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution,” Journal of Molecular Biology, vol. 175, no. 2, pp. 159–174, 1984. View at Google Scholar · View at Scopus
  24. M. Ceccarelli, R. Anedda, M. Casu, and P. Ruggerone, “CO escape from myoglobin with metadynamics simulations,” Proteins, vol. 71, no. 3, pp. 1231–1236, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. M. A. Scorciapino, A. Robertazzi, M. Casu, P. Ruggerone, and M. Ceccarelli, “Breathing motions of a respiratory protein revealed by molecular dynamics simulations,” Journal of the American Chemical Society, vol. 131, no. 33, pp. 11825–11832, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. M. A. Scorciapino, A. Robertazzi, M. Casu, P. Ruggerone, and M. Ceccarelli, “Heme proteins: the role of solvent in the dynamics of gates and portals,” Journal of the American Chemical Society, vol. 132, no. 14, pp. 5156–5163, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. B. Masala and L. Manca, “Detection of globin chains by reversed-phase high-performance liquid chromatography,” Methods in Enzymology, vol. 231, pp. 21–44, 1994. View at Publisher · View at Google Scholar · View at Scopus
  28. S. Takahashi, A. K. L. C. Lin, and C. Ho, “Proton nuclear magnetic resonance studies of hemoglobins M Boston (α58E7 His → Tyr) and M Milwaukee (β67E11 Val → Glu): spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the α and β chains of normal human adult hemoglobin,” Biochemistry, vol. 19, no. 23, pp. 5196–5202, 1980. View at Google Scholar · View at Scopus
  29. T. Y. Fang, V. Simplaceanu, C. H. Tsai, N. T. Ho, and C. Ho, “An additional H-bond in the αβ interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (βL105W),” Biochemistry, vol. 39, no. 45, pp. 13708–13718, 2000. View at Publisher · View at Google Scholar · View at Scopus
  30. V. Simplaceanu, J. A. Lukin, T. Y. Fang, M. Zou, N. T. Ho, and C. Ho, “Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin,” Biophysical Journal, vol. 79, no. 2, pp. 1146–1154, 2000. View at Google Scholar · View at Scopus
  31. M. F. Perutz, “Stereochemistry of cooperative effects in haemoglobin,” Nature, vol. 228, no. 5273, pp. 726–739, 1970. View at Publisher · View at Google Scholar · View at Scopus
  32. L. W. M. Fung and C. Ho, “A proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water,” Biochemistry, vol. 14, no. 11, pp. 2526–2535, 1975. View at Google Scholar · View at Scopus
  33. K. Ishimori, K. Imai, G. Miyazaki et al., “Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37β and 145β mutations,” Biochemistry, vol. 31, no. 12, pp. 3256–3264, 1992. View at Google Scholar · View at Scopus
  34. K. Imai, H. Morimoto, M. Kotani, S. Shibata, T. Miyaji, and K. Matsutomo, “Studies on the function of abnormal hemoglobins II. Oxygen equilibrium of abnormal hemoglobins: Shimonoseki, Ube II, Hikari, Gifu, and Agenogi,” Biochimica et Biophysica Acta, vol. 200, no. 2, pp. 197–202, 1970. View at Google Scholar
  35. R. Mojzikova, P. Dolezel, J. Pavlicek, P. Mlejnek, D. Pospisilova, and V. Divoky, “Partial glutathione reductase deficiency as a cause of diverse clinical manifestations in a family with unstable hemoglobin (Hemoglobin Haná, β63(E7) His-Asn),” Blood Cells, Molecules, and Diseases, vol. 45, no. 3, pp. 219–222, 2010. View at Publisher · View at Google Scholar