作者: Naoto Sakamoto
DOI: 10.1016/S0076-6879(78)51030-6
关键词: Escherichia coli 、 Size-exclusion chromatography 、 Chemistry 、 Biochemistry 、 Mutant 、 Perchloric acid 、 Guanine 、 Polyacrylamide gel electrophoresis 、 Dimer 、 Enzyme
摘要: Publisher Summary This chapter describes the purification procedure of guanine monphosphate synthetase (GMP) enzyme from Escherichia coli organism. The amount GMP produced is estimated by measuring increase in absorption at 290 nm reaction mixture deproteinized with perchloric acid. bacterial strain used E. B-96, a purine-requiring mutant that lacks both inosinicase and transformylase. All subsequent operations are carried out 0–4°, centrifugations performed 30,900 g for 30 min. purity preparation established data obtained disc gel electrophoresis, ultracentrifugal analyses, filtration. Polyacrylamide electrophoresis pH values 7.4 8.2 indicates preparation. apparently dimer composed identical subunits.