1970
Glutamate dehydrogenase activity in crude plant extracts
Publication
Publication
Acta botanica neerlandica , Volume 19 - Issue 3 p. 445- 453
The glutamate dehydrogenase deamination assay based on the increase of absorbance at 340 nm, caused by the transformation of NAD into NADH in the presence of L-giutamate applied to crude plant extracts, is unreliable without dialysis of the extract to eliminate disturbing reactions. A low molecular weight substance, probably a phenolic compound or aromatic amine, was isolated from Petunia leaves which could act as a substrate or activator of another dehydrogenase. This dehydrogenase which interferes with the glutamate dehydrogenase deamination assay may use many amino acids and amines as substrate. The use of a 1 % concentration of insoluble polyvinylpyrrolidone in the extraction buffer causes a higher glutamate dehydrogenase activity for both amination and deamination. The glutamate dehydrogenase is partially present in a latent form.
Additional Metadata | |
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Acta botanica neerlandica | |
CC BY 3.0 NL ("Naamsvermelding") | |
Organisation | Koninklijke Nederlandse Botanische Vereniging |
G.M.M. Bredemeijer. (1970). Glutamate dehydrogenase activity in crude plant extracts. Acta botanica neerlandica, 19(3), 445–453. |