Eur J Biochem. 1977 Aug 1;77(3):561-6.

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).

Moo-Penn WF, Schmidt RM, Jue DL, Bechtel KC, Wright JM, Horne MK 3rd, Haycraft GL, Roth EF Jr, Nagel RL.

Abstract

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.

PMID:: 19257; [PubMed - indexed for MEDLINE]

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Cited by 2 PubMed Central articles

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Hemoglobin S Travis: a sickling hemoglobin with two amino acid substitutions [be...
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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).

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