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

نویسندگان

  • J B Kwakye
  • M R Johnson
  • S Barnes
  • W E Grizzle
  • R B Diasio
چکیده

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.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Identification of bile acid coenzyme A synthetase in rat kidney.

Bile acid CoA synthetase has been discovered in rat kidney. Incubation of kidney microsomes with [14C]chenodeoxycholic acid and CoA produced a single peak with the high performance liquid chromatography (HPLC) retention time of CDC-CoA. This peak, when incubated with purified bile acid CoA: amino acid N-acyltransferase (BAT) from human liver and either taurine or glycine, led to the formation o...

متن کامل

Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.

Bile acid CoA:amino acid N-acyltransferase (BAT) is responsible for the amidation of bile acids with the amino acids taurine and glycine. Rat liver BAT (rBAT) cDNA was isolated from a rat liver lambdaZAP cDNA library and expressed in Sf9 insect cells using a baculoviral vector. rBAT displayed 65% amino acid sequence homology with human BAT (hBAT) and 85% homology with mouse BAT (mBAT). Similar ...

متن کامل

Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from rat liver.

An in vitro study of bile acid-CoA:amino acid N-acyltransferase activity of rat liver was undertaken in order to determine whether separate amino acid-specific enzymes catalyzed the formation of glycine and taurine conjugates of bile acids as postulated by others. Polyacrylamide gel electrophoresis of 200-fold purified enzyme localized the glycine- and taurine-dependent activities to a single b...

متن کامل

Peroxisomal bile acid-CoA:amino-acid N-acyltransferase in rat liver.

Bile acid-CoA:amino-acid N-acyltransferase activity was measured in subcellular fractions of rat liver homogenate. The conversion of [14C]choloyl-CoA and [14C]chenodeoxycholoyl-CoA into the corresponding [14C]tauro- and glyco-bile acids was calculated after isolation of the product by high performance liquid chromatography. There was an enrichment of bile acid-CoA:amino-acid N-acyltransferase a...

متن کامل

Acetylation of S-substituted cysteines by a rat liver and kidney microsomal N-acetyltransferase.

1. An acetyl-CoA--S-substituted cysteine N-acetyltransferase in rat liver and kidney preparations was investigated, by using an assay involving incubations with S-benzyl-L-cysteine and [l-14C]acetyl-CoA and extraction of the radioactive product with ethyl acetate. 2. The enzyme was associated with the microsomal fraction and could not be solubilized. Metal ions, EDTA and detergents did not sign...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Biochemical journal

دوره 280 ( Pt 3)  شماره 

صفحات  -

تاریخ انتشار 1991