Abstract
THE injection of tryptophan1 or cortisone3 markedly increases the tryptophan pyrrolase activity in rat liver. Tanaka and Knox3 identified this enzyme as an iron porphyrin protein. Feigelson and Greengard4 have found that addition of microsomes stimulates the tryptophan pyrrolase activity of cell sap of rat liver homogenate and that addition of hæmatin has also an activating effect. These authors suggest further that the iron porphyrin behaves as a dissociating cofactor of this enzyme5. One of us described that foetal liver cell sap6 and boiled cell saps from various organs of adult rats7 are able to elevate the tryptophan pyrrolase activity when added to the adult liver cell sap. Recently, Pitot8 has shown that manganese ions are necessary for the release of tryptophan pyrrolase from microsomes. The present work was undertaken to determine the effect of Mn2+ on the tryptophan pyrrolase activity of cell sap of rat liver homogenates.
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References
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Feigelson, P., and Greengard, O., Biochim. Biophys. Acta, 50, 200 (1961).
Chytil, F., Biochim. Biophys. Acta, 48, 217 (1961).
Chytil, F., Coll. Czechoslov. Chem. Commun. (in the press).
Pitot, H. C., and Cho, Y. S., Biochim. Biophys. Acta, 50, 197 (1961).
Knox, W. E., in Methods in Enzymology, edit. by Colowick, S. P., and Kaplan, N. O., 2, 242 (Academic Press, New York, 1955).
Mahler, H. R., in Mineral Metabolism, edit. by Comar, C. L., and Bronner, F., 1B, 743 (Academic Press, New York, 1961).
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CHYTIL, F., SKŘIVANOVÁ, J. Manganese as a Modifier of the Liver Tryptophan Pyrrolase Activity. Nature 193, 377–378 (1962). https://doi.org/10.1038/193377a0
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DOI: https://doi.org/10.1038/193377a0
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