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Hemoglobin
international journal for hemoglobin research
Volume 35, 2011 - Issue 1
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Original Article

Hb Nebraska [β86(F2)Ala→Ile (HBB:c.259G>A;260C>T)]: A Unique High Oxygen Affinity Hemoglobin Variant with a Double Nucleotide Substitution within the Same Codon

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Pages 22-27 | Received 19 Aug 2010, Accepted 13 Sep 2010, Published online: 20 Jan 2011

REFERENCES

  • Hardison RC, Chui DHK, Giardine B, et al. Hb Var: a relational database of human hemoglobin variants and thalassemia mutation at the globin gene server. Hum Mutat. 2002;19(3):225–232 (http://globin.cse.psu.edu/hbvar/menu.html).
  • Markley KM, Elkhalifa M, Maini A, Hoyer JD. Hb Jeddah [α89(E17)Asn→His (α1)]: a newly recognized α chain variant, seen in combination with Hb S [β6(A3)Glu→Val], and found in three separate families of Middle-Eastern origin. Hemoglobin. 2008;32(3):297–302.
  • Hoyer JD, Wick MJ, Thibodeau SN, Kechteiger KS, Cook JD, Fairbanks VF. Hb Silver Springs [β131(H9)Gln→His], a new hemoglobin variant found in six African-Americans. Hemoglobin. 1998;22(1):37–44.
  • Indrak K, Wiedermann BF, Batek F, Hb Olomuoc or α2β286(F2)Ala→Asp, a new high oxygen affinity variant. Hemoglobin. 1987;11(2):151–155.
  • Tagawa Y, Fujinami S, Kadota Y, Hb Olomouc [α2β286(F2)Ala→Asp] found in a Japanese family. Hemoglobin. 1992;16(1&2):73–76.
  • Pagano L, Salzano AM, Carbone V, Hb Cardarelli [β86(F2)Ala→Pro]: a new unstable and hyperaffine variant in association with β+-thalassemia. Hemoglobin. 2004;28(2):103–115.
  • Lacombe C, Craescu CT, Blouquit Y, Structural and functional studies of Hemoglobin Poissy α2β256(D7)Gly→Arg and 86(F2)Ala→Pro. Eur J Biochem. 1985,153(3):655–662.
  • Craescu CT, Schaeffer C, Blouquit Y, Rosa J. Proton NMR studies of human hemoglobin variants modified in the proximal side of β heme pocket. Implications for the affinity control and cooperative mechanism. J Biol Chem. 1988;263(7):3250–3255.

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