Khoja S M
Comp Biochem Physiol B. 1986;85(2):337-41. doi: 10.1016/0305-0491(86)90009-x.
The regulatory properties of phosphofructokinase from rat mucosa, liver, brain and muscle were investigated. Mucosal phosphofructokinase displayed cooperativity with respect to fructose 6-phosphate at pH 7.0 and so did the muscle, brain and liver isoenzymes. All these four isoenzymes were inhibited by ATP, the mucosal isoenzyme being the least inhibited. They were also inhibited by citrate and creatine phosphate. AMP, ADP, glucose 1,6-diphosphate, fructose 2,6-bisphosphate and inorganic phosphate were all strong activators for the mucosal, brain, liver and muscle phosphofructokinase, but the mucosal isoenzyme was found to be more activated than the others, accounting for the higher rates of glycolysis observed in mucosa. The results suggest that mucosal phosphofructokinase is unique and different from all the other isoenzymes.
研究了大鼠黏膜、肝脏、大脑和肌肉中磷酸果糖激酶的调节特性。黏膜磷酸果糖激酶在pH 7.0时对6-磷酸果糖表现出协同性，肌肉、大脑和肝脏的同工酶也是如此。所有这四种同工酶均受ATP抑制，其中黏膜同工酶受抑制程度最小。它们也受柠檬酸和磷酸肌酸抑制。AMP、ADP、1,6-二磷酸葡萄糖、2,6-二磷酸果糖和无机磷酸盐都是黏膜、大脑、肝脏和肌肉磷酸果糖激酶的强激活剂，但发现黏膜同工酶比其他同工酶更易被激活，这解释了在黏膜中观察到的较高糖酵解速率。结果表明，黏膜磷酸果糖激酶具有独特性，与所有其他同工酶不同。
