1.
Indian J Biochem Biophys
; 1993 Aug; 30(4): 199-203
Artículo
en Inglés
| IMSEAR
| ID: sea-29026
RESUMEN
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.
Asunto(s)
Animales , Aspartato Quinasa/aislamiento & purificación , Ensayo de Inmunoadsorción Enzimática , Epítopos/análisis , Isoenzimas/aislamiento & purificación , Cinética , Lisina/farmacología , Plantas/enzimología , Conejos/inmunología , Treonina/farmacología
2.
Indian J Biochem Biophys
; 1982 Feb; 19(1): 67-8
Artículo
en Inglés
| IMSEAR
| ID: sea-28384