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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).
W F WF Moo-Penn, R M RM Schmidt, D L DL Jue, K C KC Bechtel, J M JM Wright, M K MK Horne, G L GL Haycraft, E F EF Roth and R L RL Nagel
Eur J Biochem 77(3):561-6 (1977)
PMID 19257
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.
DOI:
Version: za2963e q8zaa q8zb6 q8zc2 q8zd7 q8ze6 q8zf6 q8zg3
DOI:
Version: za2963e q8zaa q8zb6 q8zc2 q8zd7 q8ze6 q8zf6 q8zg3