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

Academic Article

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.
  • Published In

    Keywords

  • Acyltransferases, Animals, Antibodies, Monoclonal, Chromatography, Affinity, Glycine, Glycocholic Acid, Kidney, Male, Rats, Subcellular Fractions, Substrate Specificity, Taurine, Taurocholic Acid
  • Author List

  • Kwakye JB; Johnson MR; Barnes S; Grizzle WE; Diasio RB
  • Start Page

  • 821
  • End Page

  • 824
  • Volume

  • 280 ( Pt 3)