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PLANT PHYSIOLOGY , Vol 103, Issue 1 131-137, Copyright © 1993 by American Society of Plant Biologists
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METABOLISM AND ENZYMOLOGY |
ADP/ATP Translocator from Pea Root Plastids (Comparison with Translocators from Spinach Chloroplasts and Pea Leaf Mitochondria)
D. Schunemann, S. Borchert, U. I. Flugge and H. W. Heldt
Institut fur Biochemie der Pflanze, Untere Karspule 2, 37073 Gottingen, Germany (D.S., S.B., H.W.H.)
The kinetic properties of the adenosine 5[prime]-diphosphate/adenosine
5[prime]-triphosphate (ADP/ATP) translocator from pea (Pisum sativum L.)
root plastids were determined by silicone oil filtering centrifugation and
compared with those of spinach (Spinacia oleracea L.) chloroplasts and pea
leaf mitochondria. In addition, the ADP/ATP transporting activities from
the above organelles were reconstituted into liposomes. The Km(ATP) value
of the pea root ADP/ATP translocator was 10 [mu]M and that for ADP was 46
[mu]M. Corresponding values of the spinach ADP/ATP translocator were 25
[mu]M and 28 [mu]M, respectively. Comparable results were obtained for the
reconstituted ATP transport activities. The transport was highly specific
for ATP and ADP. Adenosine 5[prime]-monophosphate (AMP) caused only a
slight inhibition and phosphoenolpyruvate and inorganic pyrophosphate
caused no inhibition of ATP uptake. With pea root plastids and spinach
chloroplasts, Km values >1 mM were obtained for ADP-glucose. Since the
concentrations of ATP and ADP-glucose in the cytosolic compartment of
spinach leaves have been determined as 2.5 and 0.6 mM, respectively, a
transport of ADP-glucose by the ADP/ATP translocator does not appear to
have any physiological significance in vivo. Although both the plastidial
and the mitochondrial ADP/ATP translocators were inhibited to some extent
by carboxyatractyloside, no immunological cross-reactivity was detected
between the plastidial and the mitochondrial proteins. It seems probable
that these proteins derive from different ancestors.
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