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Article

Hb Montfermeil [beta 130(H8) Tyr-->Cys]: suggests a key role for the interaction between helix A and H in oxygen affinity of the hemoglobin molecule.

Blood cells, molecules & diseases - 1 Jan 2000

Kister Jean, Baudin-Creuza Véronique, Kiger Laurent, Préhu Claude, Papassotiriou Ioannis, Riou Jean, Galactéros Frédéric, Wajcman Henri

Abstract excerpt

Hb Montfermeil [beta130(H8) Tyr-->Cys] is a high oxygen affinity variant causing erythrocytosis. The cysteine replacement is buried in the inside of the beta chain where it alters the interactions between helix A and H, with a further effect on helix E. This position has already been proposed to contribute to the difference in oxygen affinity between human and bovine hemoglobins. Three dimensional structural...

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Share to Amino Acid Substitution
Share to Chromatography, High Pressure Liquid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15727901
DOI: 10.1016/j.bcmd.2004.12.003

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Hb Montfermeil [beta 130(H8) Tyr-->Cys]: suggests a key role for the interaction between helix A and H in oxygen affinity of the hemoglobin molecule.PMID 15727901Read ↗

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