Abstract
1. 1. The rate of decay of the light-triggered state of ATPase in chloroplasts was decreased in the presence of Pi and accelerated by ADP in a phosphateless medium. Phosphate and arsenate inhibited the effect of ADP. 2. 2. Compared with other dinucleotides, ADP was found to be highly specific for the acceleration of the decay, having an apparent Km of 1.1·10-6 M. A lower apparent Km for ADP was obtained in the presence of phosphate. The apparent Km for the inhibition of the effect of ADP by Pi was lowered with increased concentrations of ADP. 3. 3. These and other effects on ATPase and ATP-Pi exchange activities were discussed in terms of changes in the permeability of ADP and Pi across the membrane of the chloroplast.
Original language | English |
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Pages (from-to) | 86-95 |
Number of pages | 10 |
Journal | Biochimica et Biophysica Acta - Bioenergetics |
Volume | 267 |
Issue number | 1 |
DOIs | |
State | Published - 20 Apr 1972 |