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Modification of the tyrosine hydroxylase assay

Increased enzyme activity in the presence of ascorbic acid

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Abstract

A modification of the tyrosine hydroxylase assay is described in which ascorbate, rather than 2-mercaptoethanol or dihydropteridine reductase with NADPH, is used as the reductant. Enzyme activity is 3–4 times higher with ascorbate than with the other reducing agents. Low blanks are obtained with the ascorbate system provided that catalase is also included. The tissue distribution and kinetic activation of the enzyme have been studied with the ascorbate assay. The results obtained are consistent with the biological and regulatory properties of the enzyme which have been determined with the other reducing systems.

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Author notes

  1. Pauline Lerner

    Present address: Section on Biochemistry and Pharmacology, Biological Psychiatry Branch, National Institute of Mental Health, 20014, Bethesda, Maryland

  2. Matthew M. Ames

    Present address: Department of Oncology, Mayo Clinic, 55901, Rochester, Minnesota

Authors and Affiliations

  1. Section on Biochemical Pharmacology, Hypertension-Endocrine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, 20014, Bethesda, Maryland

    Pauline Lerner, Peter Nosé, Matthew M. Ames & Walter Lovenberg

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  1. Pauline Lerner
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  2. Peter Nosé
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  3. Matthew M. Ames
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  4. Walter Lovenberg
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Lerner, P., Nosé, P., Ames, M.M. et al. Modification of the tyrosine hydroxylase assay. Neurochem Res 3, 641–651 (1978). https://doi.org/10.1007/BF00963765

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