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Mammalian histidine decarboxylase

Stability studies with special reference to the effect of salts

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Summary

Histidine decarboxylase (EC 4.1.1.22) prepared from a murine mastocytoma is activated up to six-fold when the concentration of phosphate in the assay medium is increased from 1 mM to 150 mM. Chloride and sulfate, on the other hand, are inhibitory and appear to interfere with the binding of pyridoxal phosphate to the enzyme. The inhibition by chloride is relatively less pronounced at high than at low concentrations of phosphate.

The enzyme is inhibited by heavy metal ions and to some extent by alkylation and oxidation, but also by strong reduction.

The histidine decarboxylase activity is stabilized by 150 mM potassium phosphate, 1 mM dithiothreitol and 10 μM pyridoxal phosphate when stored at 6–8 °C. This holds true for both crude extract enzyme and enzyme purified by molecular sieving and hydrophobic interaction chromatography.

Zusammenfassung

Histidin-Decarboxylase (EC 4.1.1.22), isoliert aus einem Mäuse-Mastocytom, zeigt eine bis zu sechsfach erhöhte Aktivität, wenn die Konzentration von Phosphat im Testmedium von 1 mM auf 150 mM gesteigert wird. Chlorid und Sulfat dagegen inhibieren und scheinen die Bindung von Pyridoxalphosphat an das Enzym zu verhindern. Die Inhibition von Chlorid ist bei hohen Phosphatkonzentrationen relativ geringer als bei niedrigen.

Das Enzym wird außerdem durch Schwermetallionen sowie in geringem Maße durch Alkylierung und Oxidation, aber auch durch starke Reduktion, inhibiert.

Die Histidin-Decarboxylase-Aktivität wird durch 150 mM Kaliumphosphat, 1 mM Dithiothreitol und 10 μM Pyridoxalphosphat bei 6–8°C stabilisiert. Dieses gilt sowohl für das ungereinigte als auch für das durch Gelfiltration und »Hydrophobic interaction«-Chromatographie gereinigte Enzym.

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  1. Institute of Biochemistry, University of Uppsala, Biomedical Center, Box 576, S-75123, Uppsala, Sweden

    Lena Hammar

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This work was supported by the Swedish Natural Science and Medical Research Councils, the Finsen Foundation, and the Faculty of Science, Uppsala

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Hammar, L. Mammalian histidine decarboxylase. Arch Dermatol Res 266, 285–294 (1979). https://doi.org/10.1007/BF00418574

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  • DOI: https://doi.org/10.1007/BF00418574

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