Hemoglobin Columbia Missouri or alpha 2[88 (F9) Ala----Val]beta 2: a new high-oxygen-affinity hemoglobin that causes erythrocytosis.
A previously undescribed hemoglobin variant, hemoglobin Columbia Missouri, alpha 88 (F9) Ala----Val, was detected in a 22-year-old white man who was undergoing assessment for erythrocytosis. This new hemoglobin variant does not separate from hemoglobin A by electrophoresis in conventional media, by isoelectric focusing, or by electrophoresis of purified globin chains in 8 M urea. It exhibits a high oxygen affinity, with a P50 (oxygen tension at 50% saturation) of 19.3 torr for the patient's whole blood. The substitution of hemoglobin Columbia Missouri is an internal residue near the end of the F helix of the alpha chain. Hemoglobin Okazaki has an arginyl residue substitution for a cysteinyl residue at F9 (beta 93) in the beta chain. In comparison with hemoglobin Okazaki, the substitution in hemoglobin Columbia Missouri has a more pronounced effect on oxygen affinity. Consequently, hemoglobin Columbia Missouri is associated with erythrocytosis, whereas hemoglobin Okazaki is not.
Perry
M C
MC
Department of Medicine, University of Missouri Health Sciences Center, Columbia.
Head
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C
Fairbanks
V F
VF
Jones
R T
RT
Taylor
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H
Proud
V
V
D000293:Adolescent; D000328:Adult; D001797:Blood Protein Electrophoresis; D002648:Child; D002675:Child, Preschool; D002845:Chromatography; D005260:Female; D006455:Hemoglobins, Abnormal / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D006801:Humans; D007525:Isoelectric Focusing; D008297:Male; D008875:Middle Aged; D010375:Pedigree; D011086:Polycythemia / Q000097:blood* / Q000235:genetics
D006455:Hemoglobins, Abnormal; C066860:hemoglobin Columbia Missouri