论文部分内容阅读
丙酮酸激酶(pyruvate kinase,PK,EC2.7.1.40)又称三磷酸腺苷、丙酮酸2-O-磷酸转移酶,是调节糖酵解的3个限速酶之一。PK在有锰离子和镁离子存在情况下催化磷酸烯醇式丙酮酸生成丙酮酸,这一原理被用来测定血清钾离子浓度。为了证实PK活性与血清阳离子之间的关系,特别是确定与此酶活性有关的无机离子,我们进行了PK的离子激活研究,测定钾、钠、钙、锂、锰、氨和镁7种离子对PK活性的影响。由于PK的反应产物丙酮酸并不能直接指示PK活性,因而需偶联LDH系统,通过测定NADH的衰减程度来间接指示PK活性。
Pyruvate kinase (PK, EC 2.7.1.40), also known as adenosine triphosphate, pyruvate 2-O-phosphotransferase, is one of the three rate-limiting enzymes that regulate glycolysis. PK catalyzes the phosphoenolpyruvate production of pyruvate in the presence of manganese and magnesium ions, a principle used to measure serum potassium concentration. In order to confirm the relationship between PK activity and serum cations, and in particular to determine the inorganic ions involved in this enzyme activity, we performed iontophoretic studies of PK and determined seven ions of potassium, sodium, calcium, lithium, manganese, ammonia and magnesium Effect on PK activity. Since pyruvate, a reaction product of PK, does not directly indicate PK activity, an LDH system needs to be coupled to indirectly indicate PK activity by measuring the degree of attenuation of NADH.