Hydration and selfassociation of haemoglobin in solution

The hydration of haemoglobin was determined by the nmr-freezing technique. There is a hydration-threshold around 15 mM(haem)/L, with the maximum hydration of ∼ 0.46 g H 2O/g Hb. The phosphate buffered solutions show a completely different behaviour from the other ionic and deionized solutions. The r...

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Published inBiochemical and biophysical research communications Vol. 83; no. 3; pp. 1048 - 1054
Main Authors Brnjas-Kraljević, Jasminka, Maričić, Siniša
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 14.08.1978
Subjects
Hemoglobins
Humans
Hydrogen Bonding
Kinetics
Macromolecular Substances
Magnetic Resonance Spectroscopy
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Summary:The hydration of haemoglobin was determined by the nmr-freezing technique. There is a hydration-threshold around 15 mM(haem)/L, with the maximum hydration of ∼ 0.46 g H 2O/g Hb. The phosphate buffered solutions show a completely different behaviour from the other ionic and deionized solutions. The results in ordinary water and in the presence of 80% 2H 2O are indistin-guishable. The hydration is neither a function of the extremes in the ionic double layer structure nor of the type of ions. The threshold Hb-concentration does not depend on the absolute amount of hydration and the type of ion. The results corroborate the selfassociation of haemoglobin in concentrated solutions.
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(78)91501-2