Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 26, 2002 - Issue 1
81
Views
5
CrossRef citations to date
0
Altmetric
Original

Hb SIAM [α15(A13)Gly → Arg (α1) (GGT → CGT)] IS A TYPICAL α CHAIN HEMOGLOBINOPATHY WITHOUT AN α-THALASSEMIC EFFECT

, , , , , , , & show all
Pages 77-81 | Received 19 Jun 2001, Accepted 21 Aug 2001, Published online: 07 Jul 2009

REFERENCES

  • Pootrakul S., Srichayanont S., Wasi P., Suanpan S. Hemoglobin Siam (α215Argβ2): a new α-chain variant. Hum. Genet. 1974; 23: 199–204
  • Vella F., Casey R., Lehmann H., Labossiere A., Jones T. G. Hemoglobin Ottawa: α215(A13)Gly → Argβ2. Biochim. Biophys. Acta 1974; 336: 25–29
  • Yodsowan B., Svasti J., Srisomsap C., Winichagoon P., Fuchareon S. Hb Siam [α15(A13)Gly → Arg] is a GGT → CGT mutation in the α1-globin gene. Hemoglobin 2000; 24(1)71–75
  • Orkin S. H., Goff S. C. The duplicated human α-globin genes: their selection expression as measured by RNA analysis. Cell 1981; 24: 345–351
  • Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.USA 1989
  • Chang J. C., Kan Y. W. β0 Thalassemia, a nonsense mutation in man. Proc. Natl. Acad. Sci. USA 1979; 76: 2886–2889
  • Liebhaber S. A., Cash F. E., Main D. M. Compensatory increase in α1-globin gene expression in individuals heterozygous for the α-thalassemia 2 gene deletion. J. Clin. Invest. 1985; 76: 1057–1064
  • Mrabet N., McDonald M. J., Turci S., Sarkar R., Szabo A., Bunn H. F. Electrostatic interaction governs the dimer assembly of human hemoglobin. J. Biol. Chem. 1986; 261: 5222–5228
  • Old J. M., Higgs D. R. The thalassemias; gene analysis. Methods Hematol. 1983; 6: 74–102
  • Fucharoen S., Winichagoon P., Thonglairuam V. β-Thalassemia associated with α-thalassemia in Thailand. Hemoglobin 1988; 12(5&6)581–592

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.