The adenylate kinase of human plasma, erythrocytes and platelets in relation to the degradation of adenosine diphosphate in plasma

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Abstract
Adenylate kinase (EC 2.7.4. 3) has been shown to be present in human plasma obtained by conventional means and the adenylate-kinase activities of plasma and of lysed and intact human platelets and erythrocytes have been measured at 37 degrees by sensitive spectrophotometric methods. The activities found in plasma ranged from 2.7 to 22. 9 [mu]moles of ADP formed/min/l and in lysed platelets and lysed erythrocytes mean values of 0.79 and 12.0 [mu] moles of ADP formed/min/109 cells respectively were found. Intact platelets and erythrocytes showed little or no activity. The apparent Km of plasma adenylate kinase for ADP was found to be 1.4 [long dash]1. 6mM. The adenylate-kinase activity of plasma was correlated with the free haemoglobin present and the larger part of the activity could be accounted for by haemolysis occurring either during the withdrawal of the blood or in vivo. Aggregation of platelets by ADP, collagen fibres or thrombin released up to 16 percent of the platelet adenylate kinase into the suspending medium. Measurement of the rate of breakdown of 1. 6 M-ADP in plasma gave values of about 0.1 [mu]mole/ min/ml. This was not increased by addition of sufficient erythrocyte lysate to increase the activity of plasma adenylate kinase five to ten times. It was concluded that the activity of adenylate kinase found in plasma, even after aggregation of the platelets, is insufficient to account for the rate of breakdown of low concentrations of ADP usually observed, and that another enzyme is responsible for this process.