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Crystallization and preliminary X-ray structural studies of hemoglobin A2 and hemoglobin E, isolated from the blood samples of beta-thalassemic patients.

Dasgupta J, Sen U, Choudhury D, Datta P, Chakrabarti A, Chakrabarty SB, Chakrabarty A, Dattagupta JK
Biochem Biophys Res Commun 303 619-23 (2003)
Cited: 10 times
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Abstract

Hemoglobin A(2) (alpha(2)delta(2)), a minor (2-3%) component of circulating red blood cells, acts as an anti-sickling agent and its elevated concentration in beta-thalassemia is a useful clinical diagnostic. In beta-thalassemia major, where there is a failure of beta-chain production, HbA(2) acts as the predominant oxygen delivery mechanism. Hemoglobin E, is another common abnormal hemoglobin, caused by splice site mutation in exon 1 of beta globin gene, when combines with beta-thalassemia, causes severe microcytic anemia. The purification, crystallization, and preliminary structural studies of HbA(2) and HbE are reported here. HbA(2) and HbE are purified by cation exchange column chromatography in presence of KCN from the blood samples of individuals suffering from beta-thalassemia minor and E beta-thalassemia. X-ray diffraction data of HbA(2) and HbE were collected upto 2.1 and 1.73 A, respectively. HbA(2) crystallized in space group P2(1) with unit cell parameters a=54.33 A, b=83.73 A, c=62.87 A, and beta=99.80 degrees whereas HbE crystallized in space group P2(1)2(1)2(1) with unit cell parameters a=60.89 A, b=95.81 A, and c=99.08 A. Asymmetric unit in each case contains one Hb tetramer in R(2) state.

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  1. Structural and functional studies indicating altered redox properties of hemoglobin E: implications for production of bioactive nitric oxide. Roche CJ, Malashkevich V, Balazs TC, Dantsker D, Chen Q, Moreira J, Almo SC, Friedman JM, Hirsch RE. J Biol Chem 286 23452-23466 (2011)
  2. Oxidative instability of hemoglobin E (β26 Glu→Lys) is increased in the presence of free α subunits and reversed by α-hemoglobin stabilizing protein (AHSP): Relevance to HbE/β-thalassemia. Strader MB, Kassa T, Meng F, Wood FB, Hirsch RE, Friedman JM, Alayash AI. Redox Biol 8 363-374 (2016)
  3. Dynamics based clustering of globin family members. Tobi D. PLoS One 13 e0208465 (2018)


Articles citing this publication (6)

  1. Poly(ADP-ribose) polymerase contributes to the development of myocardial infarction in diabetic rats and regulates the nuclear translocation of apoptosis-inducing factor. Xiao CY, Chen M, Zsengellér Z, Szabó C. J Pharmacol Exp Ther 310 498-504 (2004)
  2. The effects of deferiprone and deferasirox on the structure and function of beta-thalassemia hemoglobin. Moosavi-Movahedi AA, Mousavy SJ, Divsalar A, Babaahmadi A, Karimian K, Shafiee A, Kamarie M, Poursasan N, Farzami B, Riazi GH, Hakimelahi GH, Tsai FY, Ahmad F, Amani M, Saboury AA. J Biomol Struct Dyn 27 319-339 (2009)
  3. A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans. Yuan Y, Shen TJ, Gupta P, Ho NT, Simplaceanu V, Tam TC, Hofreiter M, Cooper A, Campbell KL, Ho C. Biochemistry 50 7350-7360 (2011)
  4. Differential thermal stability and oxidative vulnerability of the hemoglobin variants, HbA2 and HbE. Chakrabarti A, Bhattacharya D, Deb S, Chakraborty M. PLoS One 8 e81820 (2013)
  5. Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility. Marchany-Rivera D, Smith CA, Rodriguez-Perez JD, López-Garriga J. J Inorg Biochem 207 111055 (2020)
  6. Purification, characterization, and crystallization of Crocodylus siamensis hemoglobin. Jandaruang J, Siritapetawee J, Songsiriritthigul C, Preecharram S, Azuma T, Dhiravisit A, Fukumori Y, Thammasirirak S. Protein J 33 377-385 (2014)


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