Yamazaki T, Hara M, Kurihara Y, Kodaka S, Nakai K, Ozaki I, Sugiya H, Furuyama S
J Nihon Univ Sch Dent. 1989 Mar;31(1):366-71. doi: 10.2334/josnusd1959.31.366.
ATP-dependent profiles of phosphofructokinase (PFK) activity were determined in both crude and Sephadex G-25-filtered fractions from rabbit dental pulp. ATP had a dual effect on PFK as an activator and an inhibitor, according to its concentration. Gel-filtered PFK showed a similar profile to that of crude PFK, indicating a lack of low-molecular-weight effector(s) for PFK in rabbit dental pulp. For complete inhibition of the PFK in rabbit dental pulp, 5 mM ATP was required. This level of ATP is much higher than that required for other typical isozymes of PFK from liver, skeletal muscle or brain. It is postulated that differences in the properties of PFK isozymes are due not only to the subunit structure but also to the presence of other effectors.
测定了兔牙髓粗提物和经葡聚糖凝胶G - 25过滤的组分中磷酸果糖激酶（PFK）活性的ATP依赖性图谱。根据ATP的浓度，它对PFK具有激活剂和抑制剂的双重作用。凝胶过滤后的PFK呈现出与粗提物中PFK相似的图谱，表明兔牙髓中不存在PFK的低分子量效应物。要完全抑制兔牙髓中的PFK，需要5 mM的ATP。这个ATP水平远高于肝脏、骨骼肌或脑等其他典型PFK同工酶所需的水平。据推测，PFK同工酶性质的差异不仅归因于亚基结构，还归因于其他效应物的存在。
