title: [Purification and properties of glutamate dehydrogenase from Pseudomonas pseudoalcaligenes].
abstract: Glutamate dehydrogenase was purified from the crude extract of Pseudomonas pseudoal-caligenes. The enzyme had a molecular weight of 290,000 and was composed of six subunits with identical molecular weight of 47,000. The enzyme was highly specific for NADP(H) and the substrates. The biochemical properties such as kinetic parameters and heat stability were also examined. The purified GDH showed considerable loss of activity upon freezing.
authors.affiliation: Institute of Bioengineering, Sichuan University, Chengdu 610064.
authors.forename: S
authors.initials: S
authors.lastname: Ding
authors.forename: Z
authors.initials: Z
authors.lastname: Yang
authors.forename: Y
authors.initials: Y
authors.lastname: Tang
authors.forename: R
authors.initials: R
authors.lastname: Jing
authors.forename: S
authors.initials: S
authors.lastname: Liu
mesh_terms: D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D044205:Pseudomonas pseudoalcaligenes / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D005969:Glutamate Dehydrogenase