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Development of a sensitive and specific assay for <jats:italic>p<\/jats:italic>\u2010tyrosine decarboxylase has permitted demonstration of this activity in rat tissues and human kidney. Tyrosine decarboxylase was purified to electrophoretic homogeneity by pH 5.0 precipitation, ammonium sulfate precipitation, gel filtration, phenyl\u2010Sepharose chromatography, DEAE\u2010Sephacel chromatography, and preparative isoelectric focusing. A specific rabbit antiserum to tyrosine decarboxylase was also obtained. Purified tyrosine decarboxylase possessed a narrow pH dependency with an optimum at 8.0. Benzene and certain other organic solvents dramatically stimulated tyrosine decarboxylase activity of purified enzyme. Purified tyrosine decarboxylase activity also decarboxylated L\u2010DOPA, 5\u2010hydroxytryptophan, 3,4\u2010dihydroxyphenylserine, <jats:italic>o<\/jats:italic>\u2010tyrosine, <jats:italic>m<\/jats:italic>\u2010tyrosine, phenylalanine, histidine, and tryptophan, which suggested that the purified enzyme was aromatic L\u2010amino acid decarboxylase. This conclusion was supported by a constant ratio of 5\u2010hydroxytryptophan decarboxylase to tyrosine decarboxylase throughout the purification scheme and by parallel immunoprecipitation of decarboxylase activities by the specific antityrosine decarboxylase antisera. Thus, we report that <jats:italic>p<\/jats:italic>\u2010tyrosine is decarboxylated by aromatic L\u2010amino acid decarboxylase and that this metabolic transformation may be an important source of <jats:italic>p<\/jats:italic>\u2010tyramine in mammalian tissues. In conclusion, neuronal tissues that synthesize catecholamines or serotonin should now be considered capable of synthesizing <jats:italic>p<\/jats:italic>\u2010tyramine and other biogenic amines.<\/jats:p>","DOI":"10.1111\/j.1471-4159.1983.tb08083.x","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T13:26:16Z","timestamp":1160054776000},"page":"992-1002","source":"Crossref","is-referenced-by-count":49,"title":["Decarboxylation of <i>p<\/i>\u2010Tyrosine: A Potential Source of <i>p<\/i>\u2010Tyramine in Mammalian Tissues"],"prefix":"10.1111","volume":"40","author":[{"given":"Ronald R.","family":"Bowsher","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David P.","family":"Henry","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,10,5]]},"reference":[{"key":"e_1_2_2_2_1","first-page":"360","article-title":"A study of the factors affecting the alumina oxide\u2010trihydroxyindole procedure tor the analysis of catecholamines","volume":"138","author":"Anton A. 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