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

Abstract

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. Copyright © 1977, Wiley Blackwell. All rights reserved