Lysine- and threonine-sensitive aspartokinase isoenzymes from spinach leaves share common antigenic determinants.
Indian J Biochem Biophys
;
1993 Aug; 30(4): 199-203
Article
Dans Anglais
| IMSEAR
| ID: sea-29026
ABSTRACT
The lysine- and threonine-sensitive isoenzymes of aspartate kinase were purified to homogeneity from spinach leaves and polyclonal antibodies were raised in rabbits. The antibodies were characterized by various immunological tests like Ouchterlonys-double-diffusion, titrations of the inhibition of enzyme activity and ELISA. The antibodies against the lysine-sensitive isoenzyme could recognise as little as 50 ng of the pure antigen protein and that against the threonine-sensitive form could recognise 200 ng of the protein in the ELISA tests. The immunological tests have also shown that the lysine and threonine sensitive isoenzymes of aspartate kinase share some common antigenic determinants and differ in others.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Plantes
/
Lapins
/
Aspartate kinase
/
Thréonine
/
Test ELISA
/
Cinétique
/
Isoenzymes
/
Animaux
/
Lysine
/
Épitopes
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
1993
Type:
Article
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