Purification of betaine-aldehyde dehydrogenase from spinach leaves and preparation of its antibody.
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.
Arakawa
K
K
Department of Agricultural Chemistry, School of Agriculture, Nagoya University, Aichi.
Takabe
T
T
Sugiyama
T
T
Akazawa
T
T
D000445:Aldehyde Oxidoreductases / Q000276:immunology / Q000302:isolation & purification*; D000906:Antibodies / Q000276:immunology*; D050728:Betaine-Aldehyde Dehydrogenase; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*
D000906:Antibodies; D000445:Aldehyde Oxidoreductases; D050728:Betaine-Aldehyde Dehydrogenase