Kruger N J, Dennis D T
Biology Department, Queen's University, Kingston, Ontario, Canada K7L 3N6.
Plant Physiol. 1985 Jul;78(3):645-8. doi: 10.1104/pp.78.3.645.
In the assay of phosphofructokinase (PFK) from endosperm of germinating castor bean (Ricinus communis L.) there is a transient stimulation of initial activity by fructose 2,6-bisphosphate. This activation is due to metabolism of a limited amount of pyrophosphate (a contaminant of commercial ATP) by PPi:fructose 6-phosphate phosphotransferase (PFP), which is present in the extract. Both this activity and the amount of pyrophosphate contamination are sufficient to account for the initial increase in apparent PFK activity. The transient burst of activity is dependent on both of the above factors. Based on studies of a similar hyperactive PFK, others have proposed that PFK and PFP may be interconverted (Balogh et al. 1984 FEBS Lett 169: 287-292). The evidence for such conversions is reinterpreted in the context of the current results.
在对萌发蓖麻籽(Ricinus communis L.)胚乳中的磷酸果糖激酶(PFK)进行测定时,果糖2,6 - 二磷酸会对初始活性产生短暂刺激。这种激活是由于提取物中存在的焦磷酸:果糖6 - 磷酸磷酸转移酶(PFP)对有限量的焦磷酸(商业ATP的污染物)进行代谢所致。该活性以及焦磷酸污染量都足以解释PFK表观活性的初始增加。活性的短暂爆发取决于上述两个因素。基于对类似的高活性PFK的研究,其他人提出PFK和PFP可能会相互转化(Balogh等人,1984年,《欧洲生物化学学会联合会快报》169:287 - 292)。在当前结果的背景下,对这种转化的证据进行了重新解释。