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- W2017529312 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." @default.
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- W2017529312 date "1977-08-01" @default.
- W2017529312 modified "2023-09-26" @default.
- W2017529312 title "Hemoglobin S Travis: a Sickling Hemoglobin with Two Amino Acid Substitutions [beta6(A3)Glutamic Acid Valine and beta 142(H20) Alanine Valine]" @default.
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- W2017529312 doi "https://doi.org/10.1111/j.1432-1033.1977.tb11699.x" @default.
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