Karelin A A
Vopr Med Khim. 1976 Sep-Oct;22(5):629-34.
Activity of enzymes responsible for creatine biosynthesis (transamidinase, EC 2.1.4.1., and guanidine acetate methyltransferase, EC 2.1.1.2.) was studied in homogenates of pancreas, kidney and liver tissue of mice in normal state and in hereditary muscle dystrophy (129/Re-dy). Simultaneously, the activity of guanidine acetate methyltransferase from liver tissue was studied after addition of glucagon and ardenaline. In normal healthy mice homogenates of liver tissue distinctly increased the activity of guanidine acetate methyltransferase if glucagon and adrenaline were used in physiological concentrations. At the advanced stage of mice hereditary myodystrophy liver homogenates lost their capacity to activate the enzyme after addition of the hormones. The data obtained suggest that adenyl cyclase is impaired in plasmatic membranes of liver tissue, which mediated, using cAMP,the transformation of hormonal signals affecting the intracellular synthesis of creatine.
在正常状态及遗传性肌肉营养不良（129/Re-dy）的小鼠中，研究了胰腺、肾脏和肝脏组织匀浆中负责肌酸生物合成的酶（转脒基酶，EC 2.1.4.1，和胍乙酸甲基转移酶，EC 2.1.1.2）的活性。同时，在添加胰高血糖素和肾上腺素后，研究了肝脏组织中胍乙酸甲基转移酶的活性。在正常健康小鼠中，如果以生理浓度使用胰高血糖素和肾上腺素，肝脏组织匀浆会明显提高胍乙酸甲基转移酶的活性。在小鼠遗传性肌营养不良的晚期，添加激素后肝脏匀浆失去了激活该酶的能力。所获得的数据表明，肝脏组织质膜中的腺苷酸环化酶受损，其利用环磷酸腺苷介导影响肌酸细胞内合成的激素信号的转化。
