Site-site heterogeneity in isocitrate lyase of castor seed endosperm: evidence from kinetics of inactivation by tetranitromethane.
Indian J Biochem Biophys
;
1989 Dec; 26(6): 386-9
Article
Dans Anglais
| IMSEAR
| ID: sea-29020
ABSTRACT
Inactivation of isocitrate lyase (native and EDTA-dialysed) by excess tetranitromethane (TNM) exhibits, biphasic kinetics, in which half of the initial activity is lost in a fast and the remaining half in a slow phase each following the pseudo-first order kinetics. Rate constants of the two phases are proportional to the TNM concentration. High succinate concentration protects the enzyme against TNM inactivation only in the slow phase without any effect on the fast phase. With the EDTA-dialysed enzyme, no such protection (against inactivation by TNM) is observed in the presence of succinate or Mg2+ ions. Addition of both these ligands together brings about protection against the slow phase (as with the native enzyme). It has been proposed that the site-site heterogeneity of isocitrate lyase is a consequence of its quaternary structure constraints.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Végétaux toxiques
/
Ricinus
/
Graines
/
Tétranitro-méthane
/
Cinétique
/
Ricinus communis
/
Isocitrate lyase
/
Oxo-acid-lyases
/
Méthane
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
1989
Type:
Article
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