Hemoglobin S Travis: a sickling hemoglobin with two amino acid substitutions [beta6(A3)glutamic acid leads to valine and beta142 (h20) alanine leads to valine).
Hb S Travis is a previously undescribed sickling hemoglobin with two amino acid substitutions in the beta chain: beta6 Glu leads to Val and beta142 Ala leads to Val. The beta6 Glu leads to 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.
D000409:Alanine; D000596:Amino Acids / Q000032:analysis; D000755:Anemia, Sickle Cell / Q000097:blood / Q000235:genetics; D005260:Female; D014644:Genetic Variation; D005971:Glutamates; D006451:Hemoglobin, Sickle; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D010100:Oxygen / Q000097:blood; D010375:Pedigree; D010446:Peptide Fragments / Q000032:analysis; D014633:Valine
D000596:Amino Acids; D005971:Glutamates; D006451:Hemoglobin, Sickle; D010446:Peptide Fragments; D014633:Valine; D000409:Alanine; D010100:Oxygen