Functional and NMR studies of Hb Sassari (Asp-126 alpha----His); role of the inter-subunit contacts in the affinity control of human hemoglobin.

doi:10.1016/0167-4838(90)90279-o

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Article

Functional and NMR studies of Hb Sassari (Asp-126 alpha----His); role of the inter-subunit contacts in the affinity control of human hemoglobin.

Biochimica et biophysica acta - 5 Dec 1990

Bardakdjian-Michau J, Galactéros F, Craescu C T

Abstract excerpt

The oxygen affinity of hemoglobin Sassari (Asp-126 alpha----His), a variant substituted in the alpha 1 beta 1 interface, was found to be 8-times greater relative to normal adult human hemoglobin. Study of the exchangeable hydrogen-bonded protons by NMR spectroscopy shows only minor changes at the...

Topics

Carboxyhemoglobin
Hemoglobin A
Hemoglobins, Abnormal
Humans
Hydrogen Bonding
Hydrogen-Ion Concentration
Macromolecular Substances
Magnetic Resonance Spectroscopy
Models, Molecular
Mutation
Oxygen
Oxyhemoglobins

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Identifiers

PMID: 2268670
DOI: 10.1016/0167-4838(90)90279-o

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2268670-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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