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 language | English (US) |
|---|---|
| Pages (from-to) | 821-824 |
| Number of pages | 4 |
| Journal | Biochemical Journal |
| Volume | 280 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1991 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology