Literature DB >> 44212

N-acylation of tyramines: purification and characterization of an arylamine N-acetyltransferase from rat brain and liver.

P H Yu, A A Boulton.   

Abstract

The N-acylation of tyramine isomers and other biogenic amines has been studied. The liver exhibits the highest activity towards tyramines, while the brain exhibits a low but significant activity. In the brain, tyramine N-acylation activity was heterogenously distributed. The arylamine N-acetyltransferase has been partially purified from both rat liver and brain, the two enzymes being quite similar with respect to their chromatographic properties, optimal pH requirement (pH 7.8), and their kinetic parameters. The product N-acetyltyramine is not oxidized by liver amidohydrolase or monoamine oxidase.

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Year:  1979        PMID: 44212     DOI: 10.1139/o79-157

Source DB:  PubMed          Journal:  Can J Biochem        ISSN: 0008-4018


  2 in total

1.  Purification and properties of the enzyme arylamine N-acetyltransferase from the housefly Musca domestica.

Authors:  D P Whitaker; M W Goosey
Journal:  Biochem J       Date:  1993-10-01       Impact factor: 3.857

2.  Evaluation of the diagnostic potential of urinary N-Acetyltyramine-O,β-glucuronide (NATOG) as diagnostic biomarker for Onchocerca volvulus infection.

Authors:  Ole Lagatie; Emmanuel Njumbe Ediage; Linda Batsa Debrah; Luc Diels; Christ Nolten; Petra Vinken; Alex Debrah; Lieve Dillen; Steven Silber; Lieven J Stuyver
Journal:  Parasit Vectors       Date:  2016-05-23       Impact factor: 3.876

  2 in total

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