Abstract
Pyruvate kinase activity was determined by recording changes in pH and by recording titration of the hydroxyl ions released during the reaction. The same methods were also employed for determination of ADP and of phosphoenolpyruvate. The results obtained in the determination of pyruvate kinase activity by following the pH changes and by titration were compared to those obtained by the spectroscopic method using lactate dehydrogenase and NADH.
Original language | English |
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Pages (from-to) | 309-312 |
Number of pages | 4 |
Journal | Analytical Biochemistry |
Volume | 38 |
Issue number | 2 |
DOIs | |
State | Published - Dec 1970 |