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Histidine decarboxylase from rat and rabbit brain: Partial purification and characterization

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Abstract

Histidine decarboxylase, the synthetic enzyme for histamine, was partially purified from regions of rat or rabbit brain rich in the enzyme. The enzyme was purified using ion exchange and hydrophobic column chromatography and chromatofocusing. Approximately 70-fold and 110-fold enrichments were attained from rat and rabbit brain, respectively. Rat and rabbit brain histidine decarboxylase had isoelectric points of pH 5.4 and 5.6, Km values of 80 μM and 120 μM histidine and Vmax values of 210 and 625 pmol histamine formed/hr-mg protein, respectively. The partially purified histidine decarboxylase from both sources was dependent on pyridoxal phosphate for maximal activity and was inhibited by α-fluoromethylhistidine, nickel chloride and cobaltous chloride but was not inhibited by impromidine, α-methyldopa, DTNB, zinc chloride or mercuric chloride. The enzyme had a broad pH optimum between pH 7.2 and 8.0. These studies provide further information on the characteristics of mammalian histidine decarboxylase from brain.

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Authors and Affiliations

  1. Department of Pharmacology, University of Nebraska Medical Center, 42nd and Dewey Ave, 68105-1065, Omaha, NE

    Patricia J. Chudomelka & L. Charles Murrin

  2. Department of Biochemistry, University of Nebraska Medical Center, 42nd and Dewey Ave, 68105-1065, Omaha, NE

    Robert F. Ramaley

  3. Section of Neurology, Department of Internal Medicine, University of Nebraska Medical Center, 42nd and Dewey Ave, 68105-1065, Omaha, NE

    L. Charles Murrin

Authors
  1. Patricia J. Chudomelka
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  2. Robert F. Ramaley
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  3. L. Charles Murrin
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Chudomelka, P.J., Ramaley, R.F. & Murrin, L.C. Histidine decarboxylase from rat and rabbit brain: Partial purification and characterization. Neurochem Res 15, 17–24 (1990). https://doi.org/10.1007/BF00969179

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