A calorimetric study of the recombination of the isolated α and β chains of human hemoglobin

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Abstract

The enthalpy change accompanying recombination of αSHO2 and βSHO2 chains of human hemoglobin has been measured calorimetrically.

The overall process is exothermal, with a minimal ΔH in the neighborhood of −7000 cal/mole (of dimer).

This value appears to be somewhat dependent on the molar ratio of αSHO2 and βSHO2 chains.

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Present address: U.S. Department of Agriculture, Southern Utilization Research and Development Division of New Orleans, U.S.A.

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