Br Med J. 1975 Oct 25;4(5990):200-2.

Haemoglobin Rahere (beta Lys-Thr): A new high affinity haemoglobin associated with decreased 2, 3-diphosphoglycerate binding and relative polycythaemia.

Lorkin PA, Stephens AD, Beard ME, Wrigley PF, Adams L, Lehmann H.

Abstract

A new haemoglobin with increased oxygen affinity, beta82 (EF6) lysine leads to threonine (Hb Rahere), was found during the investigation of a patient who was found to have a raised haemoglobin concentration after a routine blood count. The substitution affects one of the 2, 3-diphosphoglycerate binding sites, resulting in an increased affinity for oxygen, but both the haem-haem interaction and the alkaline Bohr effect are normal in the haemolysate. This variant had the same mobility as haemoglobin A on electrophoresis at alkaline pH but was detected by measuring the whole blood oxygen affinity; it could be separated from haemoglobin A, however, by electrophoresis in agar at acid pH. The raised haemoglobin concentration was mainly due to a reduction in plasma volume (a relative polycythaemia) and was associated with a persistently raised white blood count. This case emphasises the need to measure the oxygen affinity of haemoglobin in all patients with absolute or relative polycythaemia when some obvious cause is not evident.

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Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met). [Acta Haematol. 1976]
Hb Helsinki: a variant with a high oxygen affinity and a substitution at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).
Ikkala E, Koskela J, Pikkarainen P, Rahiala EL, El-Hazmi MA, Nagai K, Lang A, Lehmann H. Acta Haematol. 1976; 56(5):257-75.
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Cited by 3 PubMed Central articles

Hemoglobin Rahere, a human hemoglobin variant with amino acid substitution at the 2,3-diphosphoglycerate binding site. Functional consequences of the alteration and effects of bezafibrate on the oxygen bindings. [J Clin Invest. 1985]
Hemoglobin Rahere, a human hemoglobin variant with amino acid substitution at the 2,3-diphosphoglycerate binding site. Functional consequences of the alteration and effects of bezafibrate on the oxygen bindings.
Sugihara J, Imamura T, Nagafuchi S, Bonaventura J, Bonaventura C, Cashon R. J Clin Invest. 1985 Sep; 76(3):1169-73.
High affinity haemoglobins. [Br Med J. 1977]
High affinity haemoglobins.
. Br Med J. 1977 Oct 22; 2(6094):1040-1.
Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport. [J Clin Invest. 1977]
Postsynthetic deamidation of hemoglobin Providence (beta 82 Lys replaced by Asn, Asp) and its effect on oxygen transport.
Charache S, Fox J, McCurdy P, Kazazian H Jr, Winslow R, Hathaway P, van Beneden R, Jessop M. J Clin Invest. 1977 Apr; 59(4):652-8.

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Haemoglobin Rahere (beta Lys-Thr): A new high affinity haemoglobin associated with decreased 2, 3-diphosphoglycerate binding and relative polycythaemia.

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