Pontremoli S, Melloni E, Salamino F, Sparatore B, Michetti M, Horecker B L
Proc Natl Acad Sci U S A. 1979 Dec;76(12):6323-5. doi: 10.1073/pnas.76.12.6323.
The activity of fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) in livers of fasted rabbits decreases to less than one-half the value found in livers of fed rabbits. However, the concentration of aldolase protein in the liver extracts, measured with a specific antibody, remains unchanged. More than twice as much antibody is required to neutralize the aldolase activity in liver extracts from fasted compared with fed rabbits. The results suggest that modification of liver aldolase occurs during fasting, resulting in loss of catalytic activity without loss of immunoreactivity.
禁食兔子肝脏中果糖-1,6-二磷酸醛缩酶（D-果糖-1,6-二磷酸D-甘油醛-3-磷酸裂解酶，EC 4.1.2.13）的活性降至喂食兔子肝脏中该酶活性值的一半以下。然而，用特异性抗体测定的肝脏提取物中醛缩酶蛋白的浓度保持不变。与喂食兔子相比，需要两倍多的抗体才能中和禁食兔子肝脏提取物中的醛缩酶活性。结果表明，禁食期间肝脏醛缩酶发生了修饰，导致催化活性丧失但免疫反应性未丧失。
