The role of metal ions in the uptake of aspartate aminotransferase and malate dehydrogenase into isolated rat liver mitochondria in vitro.
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.
D014013:1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt / Q000494:pharmacology; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D001693:Biological Transport, Active / Q000187:drug effects; D003035:Cobalt / Q000494:pharmacology; D007527:Isoenzymes / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D013050:Spectrometry, Fluorescence
D007527:Isoenzymes; D008670:Metals; D003035:Cobalt; D014013:1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt; D008291:Malate Dehydrogenase; D001219:Aspartate Aminotransferases