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

Biochem J. 1991 Dec 15;280 ( Pt 3)(Pt 3):821-4. doi: 10.1042/bj2800821.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyltransferases / immunology
  • Acyltransferases / isolation & purification*
  • Animals
  • Antibodies, Monoclonal
  • Chromatography, Affinity
  • Glycine / metabolism
  • Glycocholic Acid / biosynthesis
  • Kidney / enzymology*
  • Male
  • Rats
  • Subcellular Fractions / enzymology
  • Substrate Specificity
  • Taurine / metabolism
  • Taurocholic Acid / biosynthesis

Substances

  • Antibodies, Monoclonal
  • Taurine
  • Taurocholic Acid
  • Acyltransferases
  • bile acid-CoA amino acid N-acyltransferase
  • Glycocholic Acid
  • Glycine