Involvement of adenylate kinase in phosphorylation of ribose-5-phosphate by adenosinediphosphate in mitochondria-free preparations from rough lemon leaves

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Abstract
Both CO2 fixation studies and measurement of adenylate phosphate end products indicated an adenylate kinase to be the mechanism whereby adenosinetriphosphate was formed from adenosinediphosphate. Inorganic phosphate, glucose-6-phosphate, acetyl phosphate, and creatinophosphate were inactive phosphorylating agents. The results also indicated a number of phosphatases to be present in the system.