Lappin T R, Elder G E, Savage G A, Cooke P J, Bridges J M
Br J Haematol. 1982 May;51(1):73-80. doi: 10.1111/j.1365-2141.1982.tb07291.x.
In pyruvate kinase (PK)-deficient blood with high levels of reticulocytes, the degree of haemolysis after incubation at 37 degrees C for 48 h was halved by the inclusion of adenine in the medium. the decrease in haemolysis was associated with a higher ATP level but was not related to the pH of the incubation mixture. The incorporation of adenine into nucleotides studied over a 3 h period was similar in normal and PK-deficient blood. The observed increase in cellular ATP was equivalent to that shown by radioactive measurements to have been synthesized from added adenine. Inhibition of mitochondrial oxidative phosphorylation in the reticulocytes of the PK-deficient blood by KCN reduced the amount of adenine taken up by the cells by a factor of 3 and altered the pattern of incorporation into the nucleotides. Only 25% of the adenine which entered the blood cells was converted into ATP compared with 85% in the absence of cyanide. Despite the synthesis of small amounts of ATP from labelled adenine, the overall ATP content fell to less than 50% of its original level. It is suggested that incubation with adenine increased the ATP level in the reticulocytes by virtue of mitochondrial oxidative phosphorylation thereby reducing the haemolysis of these cells.
在网织红细胞水平较高的丙酮酸激酶（PK）缺乏的血液中，在培养基中加入腺嘌呤后，37℃孵育48小时后的溶血程度减半。溶血的减少与较高的ATP水平有关，但与孵育混合物的pH值无关。在3小时内对正常血液和PK缺乏血液中腺嘌呤掺入核苷酸的情况进行研究，结果相似。观察到的细胞内ATP的增加量与放射性测量结果显示的由添加的腺嘌呤合成的ATP量相当。用KCN抑制PK缺乏血液中网织红细胞的线粒体氧化磷酸化，使细胞摄取的腺嘌呤量减少了三分之一，并改变了腺嘌呤掺入核苷酸的模式。与不存在氰化物时85%的转化率相比，进入血细胞的腺嘌呤只有25%转化为ATP。尽管从标记的腺嘌呤合成了少量ATP，但总体ATP含量降至其原始水平的不到50%。有人认为，与腺嘌呤一起孵育可通过线粒体氧化磷酸化提高网织红细胞中的ATP水平，从而减少这些细胞的溶血。
