Gupta S K, Rothstein M
Biochim Biophys Acta. 1976 Oct 11;445(3):632-44. doi: 10.1016/0005-2744(76)90116-9.
Phosphoglycerate kinase (ATP:3-phospho-D-glycerate-1-phosphotransferase, EC 2.7.2.3) from young and old Turbatrix aceti has been purified to homogeneity. The "old" enzyme exhibits a marked reduction in specific activity both in crude homogenates and in pure form when compared to preparations from young nematodes. The specific activities for pure "young" and "old" enzymes are 650-750 and 300-400 units/mg, respectively. All other properties of "young" and "old" enzymes were nearly identical, including molecular weight (43 000), Km, behavior on columns, thermal stability and mobility during gel electrophoresis at three pH values. The results are discussed in terms of the possible mechanism of formation of "altered" enzymes. In addition, certain properteis of the nematode phosphoglycerate kinase are compared with those of the enzyme from yeast and rabbit muscle.
已将来自幼年和老年醋线虫的磷酸甘油酸激酶（ATP：3-磷酸-D-甘油酸-1-磷酸转移酶，EC 2.7.2.3）纯化至同质。与来自幼年线虫的制剂相比，“老年”酶在粗匀浆和纯形式下的比活性均显著降低。纯“幼年”和“老年”酶的比活性分别为650 - 750和300 - 400单位/毫克。“幼年”和“老年”酶的所有其他特性几乎相同，包括分子量（43000）、Km、在柱上的行为、热稳定性以及在三个pH值下凝胶电泳期间的迁移率。根据“改变的”酶形成的可能机制对结果进行了讨论。此外，还将线虫磷酸甘油酸激酶的某些特性与来自酵母和兔肌肉的酶的特性进行了比较。
