Ferreira R, Jacchieri S G
J Theor Biol. 1984 May 21;108(2):191-201. doi: 10.1016/s0022-5193(84)80065-x.
It is shown that the mean allosteric free energy G0(34,12) measures cooperative dioxygen binding in tetrameric hemoglobins. For human hemoglobin G0(34,12) is slightly temperature enhanced between 10 and 35 degrees C. This remarkable thermal behaviour depends on the presence in Hb of two functionally non-equivalent chains. It is proposed that this made the existence of alpha 2 beta 2 hemoglobins biologically advantageous.
结果表明，平均变构自由能G0(34,12)可衡量四聚体血红蛋白中氧结合的协同性。对于人血红蛋白，G0(34,12)在10至35摄氏度之间随温度略有升高。这种显著的热行为取决于血红蛋白中两条功能不等价链的存在。有人提出，这使得α2β2血红蛋白的存在具有生物学优势。
