engleski

The Haem-Accessibility to Solvent and Allosteric Effects in Different Protomers of Human Hemoglobin as Observed by Proton Magnetic Relaxation

1. The temperature dependence of the paramagneticlly 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. The addition of inositol hexaphosphate to either of the solutions increases the PMR rates, but this effect is significantly smaller for HbA2. 3. Taking into account the non- equivalent influence of alpha and beta chains on PMR rates, it is concluded that the mechanism of transfer of allosteric intormation upon binding of inositol hexaphosphate is less effective in HbA2 than in HbA0. Some implications of this finding are discussed here.

Haemoglobin ; Inositol hexaphosphate ; Proton magnetic relaxation

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