Abstract
IN their method for the determination of glutamic-oxalacetic transaminase without precipitation of protein, Mohun and Cook1conducted transamination between aspartic and α-ketoglutaric acid to glutamic and oxalacetic acid in a phosphate buffer solution of pH = 7.5. Similarly, Yatzidis2used a 2 per cent solution of dipotassium hydrogen phosphate for incubation of the system previous to determining the enzyme activity in the serum.
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References
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Cabaud, P., Leeper, R., and Wróblewski, P., Amer. J. Clin. Path., 26, 1101 (1956).
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SMOCZKIEWICZOWA, A., KUJAWA, H. Effect of Electrolytes on the Activity of Glutamic-Oxalacetic Transaminase. Nature 188, 487–488 (1960). https://doi.org/10.1038/188487b0
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DOI: https://doi.org/10.1038/188487b0
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