title: Purification and properties of betaine aldehyde dehydrogenase with high affinity for NADP from Arthrobacter globiformis.
abstract: Betaine aldehyde dehydrogenase from Arthrobacter globiformis was purified to apparent homogeneity by ammonium sulfate fractionation, followed by ion-exchange, butyl-Toyopearl and gel filtration chromatography. The enzyme was found to be a tetramer with identical 55 kDa subunits. Both NAD+ and NADP+ could be used as a cofactor for the enzyme and Michaelis constants (K(m) value) for NAD+ and NADP+ were 1075 microM and 48 microM, respectively. The enzyme was highly specific for betaine aldehyde and the K(m) value for betaine aldehyde was 36 microM.
authors.affiliation: Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, 4-101 Koyama-cho Minami, Tottori 680-8553, Japan. morinobu@muses.tottori-u.ac.jp
authors.forename: Nobuhiro
authors.initials: N
authors.lastname: Mori
authors.forename: Sayuri
authors.initials: S
authors.lastname: Fuchigami
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Kitamoto