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• W87823204 abstract "This chapter discusses a study analyzing characterization, localization and regulation of catecholamine synthesizing enzymes. In the study, aromatic L-amino acid decarboxylase (AADC) was purified from bovine adrenal glands. After immunization of rabbits with purified AADC (enzyme preparation obtained after polyacrylamide gel electrophoresis), specific antisera to AADC were obtained. Bovine AADC antiserum inhibits AADC activity from different tissues of various species. Immunochemical and immunohistochemical studies were applied to test whether the same enzyme catalyzes the decarboxylation of L-dopa and L-5-hydroxytryptophan (L-5HTP) or not. Earlier studies show that specific anti-serum directed against AADC inhibits L-Dopa and L-5HTP striatal decarboxylase activity proportionately. The immunohistochemical studies and the findings that 6-hydroxydopamine induced degeneration of the nigro-striatal dopamine pathway causes a proportional reduction in striatal L-Dopa and L-5HTP decarboxylase activity, support the hypothesis that a single enzyme catalyzes the decarboxylation of both aromatic L-amino acids in the striatum. However, the current data does not exclude the possibility that in some regions of the brain an enzyme exists which catalyzes specifically either L-Dopa or L-5HTP decarboxylation." @default.
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• W87823204 date "1973-01-01" @default.
• W87823204 modified "2023-10-16" @default.
• W87823204 title "CHARACTERISATION, LOCALISATION AND REGULATION OF CATECHOLAMINE SYNTHESIZING ENZYMES" @default.
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• W87823204 doi "https://doi.org/10.1016/b978-0-08-017922-3.50010-1" @default.
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