Abstract
The radioenzymatic assay of histamine (Snyder et al. 1966) provided a potentially specific and sensitive procedure for the measurement of histamine in small samples of biological fluids. A major advantage was that, unlike the biological or fluorometric assays, prior isolation of histamine from the sample was not required. The principle of the assay was simple. The sample was incubated with a radiolabeled methyl donor, S -adenosyl-L -methionine (SAMe) ([14C]- or [3H]methyl) and the enzyme histamine methyltransferase (EC 2.1.1.8) (HMT) in sodium phosphate buffer (pH 7.9) to convert the histamine in the sample to Nτ-[14C]- or [3H]methylhistamine. After the addition of NaOH, the radiolabeled methylhistamine was extracted from the reaction mixture into chloroform whereas the labeled donor and other reaction products remained in the aqueous phase. Because chloroform quenched the scintillation process the chloroform phase was evaporated to dryness and then scintillation cocktail was added for the assay of radioactivity.
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Beaven, M.A. (1991). Radioenzymatic Assays in Biological Fluids. In: Uvnäs, B. (eds) Histamine and Histamine Antagonists. Handbook of Experimental Pharmacology, vol 97. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75840-9_5
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DOI: https://doi.org/10.1007/978-3-642-75840-9_5
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