Abstract
THE possibility that the activation of glutamic-oxalacetic apoenzyme by synthetic pyridoxal phosphate required the presence of a metal was considered by Cammarata and Cohen1, after they had failed to reactivate the resolved transaminase to activity-levels comparable with those of unresolved preparations. Their examination of the emission spectra of ashed enzyme further suggested that magnesium or iron could possibly be involved. It has more recently been reported by Cohen2, however, that an examination of the possible relation of trace-metals to transaminase activity has not been particularly revealing.
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References
Cammarata, P. S., and Cohen, P. P., J. Biol. Chem., 193, 53 (1951).
Cohen, P. P., Symposium on Amino-Acid Metabolism, 56 (Johns Hopkins Press, Baltimore, 1955).
Beechey, R. B., and Happold, F. C., Biochem. J., 61, xx (1955).
Meister, A., Sober, H. A., and Peterson, E. A., J. Biol. Chem., 206, 89 (1954).
Krebs, H. A., and Eggleston, L. V., Biochem. J., 39, 408 (1945).
Greville, G. D., Biochem. J., 33, 718 (1939).
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HAPPOLD, F., TURNER, J. Effect of Magnesium Ions on Heart-Muscle Transaminase. Nature 179, 155–156 (1957). https://doi.org/10.1038/179155a0
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DOI: https://doi.org/10.1038/179155a0
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