Anderson L E, Goldhaber-Gordon I M, Li D, Tang X Y, Xiang M, Prakash N
Department of Biological Sciences, University of Illinois at Chicago 60607-7060, USA.
Planta. 1995;196(2):245-55. doi: 10.1007/BF00201381.
Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.
在相分配、荧光各向异性和等电聚焦实验中,可以观察到豌豆叶绿体(豌豆)甘油醛-3-磷酸脱氢酶(EC 1.2.1.13)与醛缩酶(EC 4.1.2.13)之间明显的物理相互作用。同样,在相分配和等电聚焦实验中获得的结果表明醛缩酶与磷酸丙糖异构酶(EC 5.3.1.1)之间存在物理相互作用。动力学实验表明,与醛缩酶结合的甘油醛-3-磷酸都可以作为甘油醛-3-磷酸脱氢酶的底物。这些结果与以下观点一致,即在光合二氧化碳固定过程和叶绿体糖酵解过程中,这三种酶之间存在相互作用。