Journal
HEMOGLOBIN
Volume 47, Issue 4, Pages 140-144Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/03630269.2023.2262391
Keywords
Hemoglobin; hemoglobin variant; oxygen affinity; high affinity hemoglobin; high performance liquid chromatography
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A new hemoglobin variant, Hb Raklev, characterized by the substitution of leucine with glutamine at position 75 in the beta-globin chain, was discovered. The variant showed possibly diminished 2,3-bisphosphoglycerate (2,3-BPG) sensitivity, resulting in heightened oxygen affinity. Two other variants have been reported at this location previously.
We present a new hemoglobin variant, Hb Raklev, characterized by the substitution of leucine with glutamine at position 75 in the beta-globin chain. This variant was discovered inadvertently during an HbA(1c) evaluation using high performance liquid chromatography in a symptomless 54-year-old Caucasian woman, with the same variant also identified in her 16-year-old daughter. Purification of the hemoglobin revealed possibly diminished 2,3-bisphosphoglycerate (2,3-BPG) sensitivity, which may result in heightened oxygen affinity. Notably, two variants have been previously documented at this location: the unstable Hb Atlanta and the high-affinity Hb Pasadena.
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