Uvelli D A, Fry D L, Finch C A, Babb A L
J Lab Clin Med. 1977 May;89(5):978-86.
The kinetics of the cyanate-hemoglobin reaction in normal whole blood have been investigated. The mechanism was found to be second order, irreversible, bimolecular. The influence of the temperature, pH, Po2, and Pco2 on the reaction rate constant was examined. A temperature change from 37 degrees to 42 degrees C, resulted in a 50 percent increase in the rate constant. The rate constant increased in proportion to the pH decrease, and deoxygenated whole blood was carbamylated approximately twice as fast as oxygenated blood. Carbon dioxide pressures had no influence on rates of carbamylation when a constant pH was maintained. A maximum rate constant of 3.7 M-U min.-u was obtained with conditions which were compatible with the red blood cells. This knowledge of the reaction mechanism and the influence of important system parameters on the reaction rate constant may be applied to the development of an extracorporeal system for the treatment of sickle cell anemia.
已对正常全血中氰酸盐 - 血红蛋白反应的动力学进行了研究。发现该反应机制为二级、不可逆、双分子反应。研究了温度、pH值、氧分压（Po2）和二氧化碳分压（Pco2）对反应速率常数的影响。温度从37摄氏度变化到42摄氏度，导致速率常数增加50%。速率常数与pH值降低成比例增加，且脱氧全血的氨甲酰化速度约为氧合血的两倍。当保持恒定pH值时，二氧化碳压力对氨甲酰化速率没有影响。在与红细胞相容的条件下，获得了最大速率常数3.7 M-1 min-1。对反应机制以及重要系统参数对反应速率常数的影响的了解，可应用于开发用于治疗镰状细胞贫血的体外系统。
