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Hemoglobin S Travis: a Sickling Hemoglobin with Two Amino Acid Substitutions [β6(A3)Glutamic Acid → Valine and β 142(H20) Alanine → Valine]

1977; Wiley; Volume: 77; Issue: 3 Linguagem: Inglês

10.1111/j.1432-1033.1977.tb11699.x

1432-1033

Winston F. Moo-Penn, Robert M. Schmidt, Danny L. Jue, Katherine C. Bechtel, J M Wright, McDonald K. Horne, Gordon L. Haycraft, Eugene F. Roth, Ronald L. Nagel,

Hemoglobinopathies and Related Disorders

Hb S Travis is a previously undescribed sickling hemoglobin with two amino acid substitutions in the β chain: β6 Glu → Val and β142 Ala→ Val. The β6 Glu→Val mutation imparts to Hb S Travis the characteristic properties of sickling hemoglobin, namely its association with erythrocyte sickling, the insolubility of the hemoglobin in the reduced form, and a minimum gelling concentration value identical to Hb S. Unlike Hb S, Hb S Travis exhibits an increased oxygen affinity and a decreased affinity for 2,3‐bisphosphoglycerate and inositol hexakisphosphate. In addition, the variant hemoglobin's tendency to autoxidize and its mechanical precipitability suggest that there are conformational differences between Hb S and Hb S Travis.