Determination of the Activity of Aminotransferases: Comparison of Two Buffer Systems with and without Supplementary Pyridoxal-5′-phosphate

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Abstract
A comparison was made between the aminotransferase activities of a number of human plasma or serum samples in 4 reaction media: phosphate buffer, phosphate buffer + pyridoxal-5''-phosphate, tris buffer and tris buffer + pyridoxal-5''-phosphate. The reactions were carried out in the various buffer systems on the same day at 35.degree. C on an automatic kinetic enzyme system. The highest enzymic activity of both aminotransferases was observed in tris buffer + pyridoxal-5''-phosphate. The activity was about 10-15% higher than in phosphate buffer + pyridoxal-5''-phosphate. Without supplementary pyridoxal-5''-phosphate the differences between both buffer systems were lower or absent. It appeared necessary, to determine the activity of both aminotransferases in a buffer system with tris and to add pyridoxal-5''-phosphate, since assays should be carried out in the presence of optimal concentrations of any of the necessary factors.

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