Hemoglobin Shelby [beta 131(H9) Gln----Lys] a correction to the structure of hemoglobin Deaconess and hemoglobin Leslie.
Hemoglobin Shelby, detected in two unrelated black families, has an electrophoretic mobility like Hb F on cellulose acetate (pH 8.4) and a mobility between Hbs S and C on citrate agar (pH 6.2). Globin chain analysis in acid and alkaline buffers revealed an abnormal chain migrating between beta A and beta S. Tests for unstable hemoglobins were positive. Hematologic data on both families indicated carriers have mild anemia. The variant showed a slightly lower affinity for oxygen with normal cooperativity and Bohr effect, and its reactions with 2,3-diphosphoglycerate and inositol hexaphosphate were similar to those of Hb A. Sequence analysis indicated the substitution of lysine for glutamine at position 131 in the beta-chain. In a previous report (1) we described a variant, Hb Deaconess, in which this residue was deleted. On reexamination of the data, we find that Hb Deaconess is identical to Hb Shelby.
D000293:Adolescent; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D001797:Blood Protein Electrophoresis; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006455:Hemoglobins, Abnormal / Q000032:analysis*; D006801:Humans; D007223:Infant; D008297:Male
D000596:Amino Acids; D006455:Hemoglobins, Abnormal; C044398:hemoglobin Shelby