Balíková-Bycková V, Pristach J, Vodrácka Z
Physiol Bohemoslov. 1975 Sep;24(5):403-12.
The measurements of oxidation-reduction potentials at pH 7.0 and ionic strength of 0.1 revealed only a slight difference between human adult (HbA) and foetal haemoglobin (HbF) (161 and 145 mV), which disappeared on increasing the ionic strength to 2.1. Kinetic data for the reactions with potassium ferricyanide and sodium nitrite of both haemoglobins in oxy- and carbonmonoxi-forms are presented at different excessive molar concentrations of oxidizing agents, in different environments at pH 7.0 and temperature ranging from 10--30 degrees C. The rate of HbF oxidation was considerably higher with both agents, despite vast differences in the reaction mechanisms.
在pH值为7.0、离子强度为0.1的条件下对氧化还原电位进行测量,结果显示成人血红蛋白(HbA)和胎儿血红蛋白(HbF)之间仅有细微差异(分别为161 mV和145 mV),但当离子强度增加到2.1时,这种差异消失了。本文给出了在pH值为7.0、温度范围为10 - 30摄氏度的不同环境中,两种血红蛋白的氧合形式和一氧化碳结合形式与铁氰化钾和亚硝酸钠反应时,在不同过量摩尔浓度氧化剂条件下的动力学数据。尽管反应机制存在巨大差异,但两种试剂氧化HbF的速率都显著更高。