Interaction of Chicken Liver Tropomyosin with Glutamate Dehydrogenase

Biochemical and Immunohistochemical Studies on Tropomyosin and Glutamate Dehydrogenase in the Chicken Liver

“…As demonstrated in the previous study (Akutsu et al ., 2000), chicken liver TM bound to GDH, an allosteric enzyme that catalizes transition of L-glutamate into 2-oxoglutarate (Smith et al ., 1975). 2D-PAGE of eluates obtained by TMaffinity column chromatography showed that purified chicken liver GDH directly associated with TM (Fig.…”

“…We showed in the previous study (Akutsu et al ., 2000) that GDH interacted with TM in the absence of ATP, an allosteric inhibitor of GDH enzymatic activity, but the interaction was inhibited by 0.1 mM ATP. From our previous and present results, we propose two hypotheses on physiological roles of the interaction between TM and GDH in nonmuscle cells (Fig.…”

“…It is significant to reveal the precise functional properties of TM and its associated proteins in order to elucidate the regulation of the actin cytoskeleton. We searched for novel nonmuscle TM-binding proteins from the chicken liver by affinity column chromatography and demonstrated that glutamate dehydrogenase (GDH), that plays a central roles in gluta-mate metabolism, bound to the TM in an ATP-dependent manner (Akutsu et al ., 2000), like caldesmon and calponin which associate with TM and F-actin in a Ca 2+ -dependent fashion. GDH interacted with TM in the absence of ATP, but the association was inhibited by 0.1 mM ATP.…”