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 chromatorgraphy. The enzyme was judged to consist of two identical pieces of the monomeric subunit with molecular weight of 60 kDa. A...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1987, Vol.101 (6), p.1485-1488
Main Authors: Arakawa, K, Takabe, T, Sugiyama, T, Akazawa, T
Format: Article
Language:English
Subjects:
aldehyde dehydrogenase
Aldehyde Oxidoreductases - immunology
Aldehyde Oxidoreductases - isolation & purification
Analytical, structural and metabolic biochemistry
antibodies
Antibodies - immunology
betaine
Betaine-Aldehyde Dehydrogenase
Biological and medical sciences
chloroplasts
enzyme activity
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
leaves
Molecular Weight
Oxidoreductases
Plants - enzymology
Spinacea oleracea
Spinacia oleracea
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Description
Summary: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 chromatorgraphy. 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.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122019