title: Purification of betaine-aldehyde dehydrogenase from spinach leaves and preparation of its antibody.
abstract: Betaine-aldehyde dehydrogenase was purified from spinach leaves and characterized. The molecular weight of the enzyme was estimated to be 120 kDa by a gel filtration chromatography. The enzyme was judged to consist of two identical pieces of the monomeric subunit with molecular weight of 60 kDa. A specific polyclonal antibody was raised against the enzyme subunit.
authors: Department of Agricultural Chemistry, School of Agriculture, Nagoya University, Aichi.
authors: K
authors: K
authors: Arakawa
authors: T
authors: T
authors: Takabe
authors: T
authors: T
authors: Sugiyama
authors: T
authors: T
authors: Akazawa
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000276:immunology / Q000302:isolation & purification*; D000906:Antibodies / Q000276:immunology*; D050728:Betaine-Aldehyde Dehydrogenase; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*
chemical_list: D000906:Antibodies; D000445:Aldehyde Oxidoreductases; D050728:Betaine-Aldehyde Dehydrogenase