The haem-accessibility to solvent and allosteric effects in different protomers of human haemoglobins as observed by proton magnetic relaxation

S. Vuk-Pavlović, B. Benko, S. Maričić, B. Markovska, G. D. Efremov

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

1. 1. The temperature dependence of the paramagnetically induced molar solvent-proton longitudinal magnetic relaxation (PMR) rates in the phosphate-free solutions of aquomet derivatives of human haemoglobins A0 and A2 are almost identical. 2. 2. The addition of inositol hexaphosphate to either of the solutions increases the PMR rates, but this effect is significantly smaller for HbA2. 3. 3. Taking into account the non-equivalent influence of α and β chains on PMR rates, it is concluded that the mechanism of transfer of the allosteric information upon binding of inositol hexaphosphate is less effective in HbA2 than in HbA0. Some implications of this finding are discussed here.

Original languageEnglish (US)
Pages (from-to)367-370
Number of pages4
JournalInternational Journal of Biochemistry
Volume7
Issue number8
DOIs
StatePublished - 1976

ASJC Scopus subject areas

  • Biochemistry

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