Friedrich C G, Friedrich B, Schlegel H G
Arch Microbiol. 1976 Mar 19;107(2):125-31. doi: 10.1007/BF00446831.
Properties and regulation of anthranilate synthase from Alcaligenes eutrophus H 16 were investigated. Anthranilate synthase was partially purified from crude extracts by affinity chromatography on tryptophan-substituted Sepharose, and was used for kinetic measurements. During the purification procedure the enzyme was stabilized by 50 mM L-glutamine or during chromatography on DEAE- cellulose and Sephadex G-200 with 30% glucerol, respectively.
对嗜碱假单胞菌H 16的邻氨基苯甲酸合酶的性质和调控进行了研究。通过在色氨酸取代的琼脂糖上进行亲和层析,从粗提物中部分纯化了邻氨基苯甲酸合酶,并用于动力学测量。在纯化过程中,该酶分别通过50 mM L-谷氨酰胺或在含30%甘油的DEAE-纤维素和葡聚糖G-200上进行层析来稳定。