Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange

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Bibliographic Details
Published in:FEBS letters 1977-05, Vol.77 (1), p.103-106
Main Authors: Abaturov, L.V., Jinoria, K.Sh, Varshavsky, Ya.M., Yakobashvily, N.N.
Format: Article
Language:English
Subjects:
deoxy Hb
different ligand states of ferrihemoglobin A (MetHb)
different ligand states of ferrohemoglobin A
Drug Stability
HbO2 and HbCO
Heme
hemoglobin A
Hemoglobins
Humans
Kinetics
Ligands
MetHbH2O, MetHbOH and MetHbCN
Methemoglobin
Oxyhemoglobins
Protein Binding
Protein Conformation
unliganded ferrohemoglobin A
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(77)80202-0