Table of Contents
ISRN Hematology
Volume 2013 (2013), Article ID 629640, 5 pages
http://dx.doi.org/10.1155/2013/629640
Research Article

Interaction of Normal and Sickle Hemoglobins for Sodium Dodecylsulphate and Hydrogen Peroxide at pH 5.0 and 7.2

1Department of Biochemistry, University of Nigeria, Nsukka, Enugu State, Nigeria
2Department of Biochemistry, Anambra State University, Uli, Nigeria

Received 8 July 2013; Accepted 29 August 2013

Academic Editors: A. Bosly, E. Cobos, and H. Knecht

Copyright © 2013 Fortunatus C. Ezebuo 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. P. S. Sijwali, K. Kato, K. B. Seydel et al., “Plasmodium falciparum cysteine protease falcipain-1 is not essential in erythrocytic stage malaria parasites,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 23, pp. 8721–8726, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. B. L. Tekwani and L. A. Walker, “Targeting the hemozoin synthesis pathway for new antimalarial drug discovery: technologies for in vitro β-hematin formation assay,” Combinatorial Chemistry and High Throughput Screening, vol. 8, no. 1, pp. 63–79, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Chugh, V. Sundararaman, and S. Kumar, “Protein complex directs hemoglobin-to-hemozoin formation in Plasmodium falciparum,” Proceedings of the National Academy of Sciences, vol. 110, no. 14, pp. 5392–5397, 2013. View at Google Scholar
  4. J. Prousek, “Fenton chemistry in biology and medicine,” Pure and Applied Chemistry, vol. 79, no. 12, pp. 2325–2338, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Hanspal, M. Dua, Y. Takakuwa, A. H. Chishti, and A. Mizuno, “Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development,” Blood, vol. 100, no. 3, pp. 1048–1054, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Singh, M. M. Alam, I. Pal-Bhowmick, J. A. Brzostowski, and C. E. Chitnis, “Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites,” PLoS Pathogens, vol. 6, no. 2, Article ID e1000746, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. L. Fielding, “NMR methods for the determination of protein-ligand dissociation constants,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 51, no. 4, pp. 219–242, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. K. R. Denninghoff, R. A. Chipman, and L. W. Hillman, “Oxyhemoglobin saturation measurements by green spectral shift,” Optics Letters, vol. 31, no. 7, pp. 924–926, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. L. Gebicka and E. Banasiak, “Flavonoids as reductants of ferryl hemoglobin,” Acta Biochimica Polonica, vol. 56, no. 3, pp. 509–513, 2009. View at Google Scholar · View at Scopus
  10. K. D. Vandegriff, A. Malavalli, C. Minn et al., “Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates,” Biochemical Journal, vol. 399, no. 3, pp. 463–471, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. P. Chenprakhon, J. Sucharitakul, B. Panijpan, and P. Chaiyen, “Measuring binding affinity of protein-ligand interaction using spectrophotometry: binding of neutral red to riboflavin-binding protein,” Journal of Chemical Education, vol. 87, no. 8, pp. 829–831, 2010. View at Publisher · View at Google Scholar · View at Scopus
  12. M. A. Ibrahim, M. I. El-Gohary, N. A. Saleh, and M. Y. Elashry, “Spectroscopic study on the oxidative reactions of normal and pathogenic hemoglobin molecules,” Romanian Journal Biophys, vol. 18, no. 1, pp. 39–47, 2008. View at Google Scholar
  13. K. B. Samir and M. J. Marcolina, “Hyperhemolysis during the evolution of uncomplicated acute painful episodes in patients with sickle cell anemia,” Transfusion, vol. 46, no. 1, pp. 105–110, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. F. X. Schmid, “Spectral methods of charactering protein conformation and conformational changes,” in Protein Structure: A Practical Approach, T. E. Creighton, Ed., pp. 251–284, IRL Press, New York, NY, USA, 1990. View at Google Scholar
  15. M. Matsui, A. Nakahara, A. Takatsu, K. Kato, and N. Matsuda, “Insitu observation of the state and stability of hemoglobin adsorbed onto glass surface by slab optical waveguide (SOWG) spectroscopy,” International Journal of Chemical and Biological Engineering, vol. 1, no. 2, pp. 72–75, 2008. View at Google Scholar