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Hemoglobin
international journal for hemoglobin research
Volume 27, 2003 - Issue 4
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Short Communication

Three New Hemoglobin Variants with Abnormal Oxygen Affinity: Hb Saratoga Springs [α40(C5)Lys→Asn (α1)], Hb Santa Clara [β97(FG4)His→Asn], and Hb Sparta [β103(G5)Phe→Val]

Dr. James D. Hoyer Department of Laboratory Medicine and Pathology, Mayo Clinic, 200 First St., Rochester, Minnesota, 55905, USA
,
John Weinhold Glen Falls, New YorkUSA
,
Elisabeth Mailhot Santa Clara Valley Medical Center, San Jose, CaliforniaUSA
,
David Alter Spectrum Health, Grand Rapids, MichiganUSA
,
Daniel J. McCormick Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MinnesotaUSA
,
Karen Snow Department of Laboratory Medicine and Pathology, Mayo Clinic, 200 First St., Rochester, Minnesota, 55905, USA
,
Kathleen S. Kubik Department of Laboratory Medicine and Pathology, Mayo Clinic, 200 First St., Rochester, Minnesota, 55905, USA
,
Michael W. Holmes Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MinnesotaUSA
&
Virgil F. Fairbanks Department of Laboratory Medicine and Pathology, Mayo Clinic, 200 First St., Rochester, Minnesota, 55905, USA
 show all
Pages 235-241 | Received 03 Jun 2003, Accepted 10 Jul 2003, Published online: 07 Jul 2009

References

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  • Hutt P. J., Fairbanks V. F., Thibodeau S. N., Green M. M., Hoyer J. D., Block H., Day C., Jones R. T., Barwick R. C. Hb T‐Cambodia, a β chain variant with the mutations of Hb E and Hb D‐Punjab confirmed by DNA analysis. Hemoglobin 1997; 21(3)205–218
  • Schneider R. G., Barwick R. C. Measuring relative electrophoretic mobilities of mutant hemoglobins and globin chains. Hemoglobin 1978; 2(5)417–435
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  • Fairbanks V. F., Maldonado J. E., Charache S., Boyer S. H. Familial erythrocytosis due to electrophoretically undetectable hemoglobin with impaired oxygen dissociation (Hemoglobin Malmo α2 β2 97 gln). Mayo Clin Proc 1971; 46(11)721–727
  • Taketa F., Huang Y. P., Libnoch J. A., Dessel B. H. Hemoglobin Wood β97(FG4) His→Leu. A new high‐oxygen‐affinity hemoglobin associated with familial erythrocytosis. Biochim Biophys Acta 1975; 400(2)348–353
  • Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., Shibata K., Shimokata H., Kuzuya F., Miwa S. A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or β97(FG4)His→Pro. Hemoglobin 1985; 9(1)11–24
  • Ohba Y., Imai K., Kumada I., Ohsawa A., Miyaji T. Hb Moriguchi or α2β2(97) (FG4)His→Tyr substitution at the α1‐β2 interface. Hemoglobin 1989; 13(4)367–376
  • White J. M., Szur L., Gillies I. D.S., Lorkin P. A., Lehmann H. Familial polycythaemia caused by a new haemoglobin variant: Hb Heathrow, β103 (G5) phenylalanine→leucine. Br Med J 1973; 3(5882)665–667
  • Marsh G., Marino G., Pucci P., Ferranti P., Malorni A., Kaeda J., Marsh J., Luzzatto L. A third instance of the high oxygen affinity variant, Hb Heathrow [β103(G5)Phe→Leu]: identification of the mutation by mass spectrometry and by DNA analysis. Hemoglobin 1991; 15(1&2)43–51
  • Wajcman H., Kister J., M'Rad A., Prome D., Milipied N., Rapp M. J., Harousseau J. L., Riou J., Bardakdjian J., Galacteros F. Hb Saint Nazaire (β103(G5)Phe→Ile): a new example of polycythemia due to a hemoglobin variant with increased oxygen affinity. Am J Hematol 1993; 44(1)16–21

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