Identification of bile acid-CoA: amino acid N-acyltransferase in rat kidney.
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.
Kwakye
J B
JB
Department of Pharmacology, University of Alabama, Birmingham 35294.
Johnson
M R
MR
Barnes
S
S
Grizzle
W E
WE
Diasio
R B
RB
D000217:Acyltransferases / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity; D005998:Glycine / Q000378:metabolism; D006000:Glycocholic Acid / Q000096:biosynthesis; D007668:Kidney / Q000201:enzymology*; D008297:Male; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013654:Taurine / Q000378:metabolism; D013656:Taurocholic Acid / Q000096:biosynthesis
D000911:Antibodies, Monoclonal; D013654:Taurine; D013656:Taurocholic Acid; D000217:Acyltransferases; C026953:bile acid-CoA amino acid N-acyltransferase; D006000:Glycocholic Acid; D005998:Glycine