Identification of bile acid-CoA:amino acid N-acyltransferase in rat kidney

J. B. Kwakye, M. R. Johnson, S. Barnes, W. E. Grizzle, R. B. Diasio

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

A novel location of the bile-acid-conjugating enzyme bile acid-CoA:amino acid N-acyltransferase (BAT) has been discovered in the cytosolic fraction of rat kidney. Both taurine and glycine were utilized as substrates. Formation of bile acid N-acyl amidates was verified by h.p.l.c. by comparison with authentic standards and by specific hydrolysis using cholylglycine hydrolase. Immunoblot analysis using a human liver anti-BAT polyclonal antibody indicated that rat kidney BAT has the same molecular mass as rat liver BAT. These findings suggest that the kidney has a role in bile acid metabolism and physiology.

Original languageEnglish (US)
Pages (from-to)821-824
Number of pages4
JournalBiochemical Journal
Volume280
Issue number3
DOIs
StatePublished - 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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