Bassols A, Andrés V, Ballarín M, Mahy N, Carreras J, Cussó R
Unitat de Bioquímica, Facultat de Medicina, Universitat de Barcelona, Zona Universitària Pedralbes, Spain.
Arch Biochem Biophys. 1991 Nov 15;291(1):121-5. doi: 10.1016/0003-9861(91)90113-w.
Glucose-1,6-bisphosphatase activity in rat skeletal muscle extracts was lost after exhaustive dialysis or precipitation with ammonium sulfate. Most of the original activity was recovered when the boiled extract was added to the ammonium sulfate precipitate. Qualitative analysis of the boiled extract revealed that the activator was either a nucleoside or a nucleotide. The results show that at concentrations between 0.05 and 1 mM, only guanine and adenosine derivatives are effective as activators, the former being more powerful. However, only guanosine, ADP, and AMP have an activating effect at the concentrations found in the boiled extract. The results of assays in vitro suggest that adenine nucleotides could be physiological modulators of glucose-1,6-bisphosphatase activity during muscle contraction.
大鼠骨骼肌提取物中的葡萄糖-1,6-二磷酸酶活性在彻底透析或用硫酸铵沉淀后丧失。当将煮沸的提取物加入到硫酸铵沉淀中时，大部分原始活性得以恢复。对煮沸提取物的定性分析表明，激活剂要么是核苷要么是核苷酸。结果表明，在0.05至1 mM的浓度范围内，只有鸟嘌呤和腺苷衍生物作为激活剂有效，前者作用更强。然而，在煮沸提取物中发现的浓度下，只有鸟苷、ADP和AMP具有激活作用。体外测定结果表明，腺嘌呤核苷酸可能是肌肉收缩过程中葡萄糖-1,6-二磷酸酶活性的生理调节剂。
