Tertiary conformational transition in sheep hemoglobins induced by reaction with 5,5´-dithiobis(2-nitrobenzoate) and by binding of inositol hexakisphosphate
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference42 articles.
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4. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin;Perutz;Biochemistry,1974
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1. R and R2 quaternary structures of carbonmonoxyhemoglobins: Differential effect of inositol hexakisphosphate on their affinity for Ellman's reagent;Biophysical Chemistry;2019-04
2. Bohr effect of human hemoglobin A: Magnitude of negative contributions determined by the equilibrium between two tertiary structures;Biophysical Chemistry;2014-06
3. High ionic strength or presence of inositol hexakisphosphate reverses the unusually low pKA of CYSH3(125)Β of guinea pig haemoglobin;Bulletin of the Chemical Society of Ethiopia;2012-12-15
4. The reactivity of CysF9[93]β sulphydryl group of des-HisHC3[146]β human haemoglobin A;AFRICAN JOURNAL OF BIOTECHNOLOGY;2011-10-31
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