Sandmann G, Hilgenberg W
Z Naturforsch C Biosci. 1978 Sep-Oct;33(9-10):667-70.
Phosphoenolpyruvate carboxykinase (PEPCK) from Phycomyces blakesleeanus was partially purified by protamine sulfate precipitation, ammoniumsulfate precipitation, and diethylamino ethyl cellulose (DEAE) treatment. This preparation was employed for the characterization of the enzyme. The Km values for phosphoenolpyruvate (PEP) and ADP were determined as 1.6 and 0.42 mM. The nucleotid specificity was demonstrated for ADP exclusively. The use of sulfuryl reagents showed the presence of thiol groups sensitive against p-hydroxymercuribenzoate but not effected by N-ethylmaleimide.
来自布氏根霉的磷酸烯醇式丙酮酸羧激酶(PEPCK)通过硫酸鱼精蛋白沉淀、硫酸铵沉淀和二乙氨基乙基纤维素(DEAE)处理进行了部分纯化。该制剂用于酶的特性鉴定。磷酸烯醇式丙酮酸(PEP)和ADP的米氏常数分别测定为1.6和0.42 mM。核苷酸特异性仅显示对ADP有作用。使用磺酰试剂表明存在对对羟基汞苯甲酸敏感但不受N-乙基马来酰亚胺影响的巯基。