Garcia-Olalla C, Garrido-Pertierra A
Biochem J. 1987 Jan 15;241(2):573-81. doi: 10.1042/bj2410573.
Two forms of pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 2.7.1.40) present in Salmonella typhimurium were purified to homogeneity from the same cultures by (NH4)2SO4 fractionation and gel filtration, anion-exchange and affinity chromatography. Mr values, subunit structure, amino acid composition and activity and stability conditions were determined for the two forms. Kinetic and regulatory properties of the two purified isoenzymes were studied.
通过硫酸铵分级沉淀、凝胶过滤、阴离子交换和亲和层析，从相同培养物中纯化出鼠伤寒沙门氏菌中存在的两种丙酮酸激酶（ATP：丙酮酸2-O-磷酸转移酶，EC 2.7.1.40），使其达到同质状态。测定了这两种形式的相对分子质量值、亚基结构、氨基酸组成以及活性和稳定性条件。研究了两种纯化的同工酶的动力学和调节特性。
