The role of metal ions in the uptake of aspartate aminotransferase and malate dehydrogenase into isolated rat liver mitochondria in vitro

FEBS Letters

Doonan, S.²  Atlante, A.¹  Passarella, S.¹  Quagliariello, E.¹  Marra, E.¹ 

[1] Dipartimento di Biochimica e Biologia Molecolare and Centra di Studio sui Mitocondri e Metabolismo Energetico, CNR, Universitá di Bari, Via Amendola 1651 A, 70126 Bari, Italy;Department of Biochemistry, University College, Cork, Ireland

关键词: Mitochondria;    Transport;    Asparate aminotransferase;    Malate dehydrogenase;    Metal-complexing agent;    AAT;    aspartate aminotransferase;    MDH;    malate dehydrogenase;   

DOI  :  10.1016/0014-5793(85)81030-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To gain further insight into the mitochondrial receptor area which allows selective uptake of both purified aspartate aminotransferase and malate dehydrogenase into mitochondria, the inhibition of metal complexing agents such as bathophenanthroline and tiron on the uptake of both enzymes has been investigated. In view of the nature of the inhibition found, we propose the existence of metal ion(s) at or near the aspartate aminotransferase, but far from the malate dehydrogenase binding site.

【 授权许可】

Unknown