Knull H R, Fillmore S J
Comp Biochem Physiol B. 1985;81(2):349-51. doi: 10.1016/0305-0491(85)90324-4.
The specific activities of glucosephosphate isomerase, aldolase, triosephosphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, pyruvate kinase and lactate dehydrogenase were all higher in the synaptoplasmic fraction from rat brain than in 100,000 g supernatant fraction of rat brain homogenates when the supernatants were prepared in high ionic strength solutions. Four enzymes in synaptosomes and two enzymes in homogenates were associated with particulate fractions as indicated by the large increase in specific activity of the enzymes when samples were treated with 0.3 M KCl before centrifugation. Glucosephosphate isomerase, aldolase, pyruvate kinase and lactate dehydrogenase were the enzymes that showed a large increase in specific activity following salt treatment of isolated, synaptosomal membrane while aldolase and pyruvate kinase were the two enzymes which showed a large increase in specific activity in the high speed supernatant fractions. Because the specific activities of many enzymes are found to be elevated not only in synaptosomes but in synaptosomal membrane fractions it is suggested that these enzymes may provide the potential for significantly enhanced glycolysis at these locations.
当在高离子强度溶液中制备上清液时，大鼠脑突触体部分中葡萄糖磷酸异构酶、醛缩酶、磷酸丙糖异构酶、甘油醛磷酸脱氢酶、磷酸甘油酸激酶、磷酸甘油酸变位酶、丙酮酸激酶和乳酸脱氢酶的比活性均高于大鼠脑匀浆100,000 g上清液部分。如在离心前用0.3 M KCl处理样品时酶的比活性大幅增加所示，突触体中的四种酶和匀浆中的两种酶与颗粒部分相关。葡萄糖磷酸异构酶、醛缩酶、丙酮酸激酶和乳酸脱氢酶是在分离的突触体膜经盐处理后比活性大幅增加的酶，而醛缩酶和丙酮酸激酶是在高速上清液部分比活性大幅增加的两种酶。由于发现许多酶的比活性不仅在突触体中升高，而且在突触体膜部分中也升高，因此表明这些酶可能在这些位置提供显著增强糖酵解的潜力。
