A comparative study of bile acid CoA: Amino acid:N-acyltransferase (BAT) from four mammalian species

Joseph B. Kwakye, Martin R. Johnson, Stephen Barnes, Robert B Diasio

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

1. 1. Bile acid CoA:amino acid:N-acyltransferase (BAT) was partially purified from dog, human, pig and rat livers. The interspecies variation in substrate specificity and kinetics were determined for glycine and taurine. 2. 2. BAT activity from dog liver formed bile acid conjugates with taurine exclusively, whereas BAT activity from each of the other species formed conjugates with both taurine and glycine. 3. 3. Biliary composition of glycine and taurine bile acid conjugates could partly be accounted for by substrate affinity (Km) and turnover number (Vmax) of BAT activity. 4. 4. A monospecific anti-human BAT polyclonal antibody reacted on Western blot analysis with a 40 kDa band in a 100,000 g supernatant fraction from rat liver. 5. 5. Immunoabsorption chromatography using an anti-human BAT antibody-Sepharose affinity column showed that both the immunoreactive protein band and BAT activity were removed from the 100,000 g supernatant fraction from human and rat livers.

Original languageEnglish (US)
Pages (from-to)131-136
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume100
Issue number1
DOIs
StatePublished - 1991
Externally publishedYes

Fingerprint

Taurine
Liver
Glycine
Rats
Bile Acids and Salts
Dogs
Antibody Affinity
Antibodies
Substrates
Substrate Specificity
Chromatography
Sepharose
Swine
Western Blotting
Kinetics
bile acid-CoA amino acid N-acyltransferase
Chemical analysis
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

Cite this

A comparative study of bile acid CoA : Amino acid:N-acyltransferase (BAT) from four mammalian species. / Kwakye, Joseph B.; Johnson, Martin R.; Barnes, Stephen; Diasio, Robert B.

In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 100, No. 1, 1991, p. 131-136.

Research output: Contribution to journalArticle

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N2 - 1. 1. Bile acid CoA:amino acid:N-acyltransferase (BAT) was partially purified from dog, human, pig and rat livers. The interspecies variation in substrate specificity and kinetics were determined for glycine and taurine. 2. 2. BAT activity from dog liver formed bile acid conjugates with taurine exclusively, whereas BAT activity from each of the other species formed conjugates with both taurine and glycine. 3. 3. Biliary composition of glycine and taurine bile acid conjugates could partly be accounted for by substrate affinity (Km) and turnover number (Vmax) of BAT activity. 4. 4. A monospecific anti-human BAT polyclonal antibody reacted on Western blot analysis with a 40 kDa band in a 100,000 g supernatant fraction from rat liver. 5. 5. Immunoabsorption chromatography using an anti-human BAT antibody-Sepharose affinity column showed that both the immunoreactive protein band and BAT activity were removed from the 100,000 g supernatant fraction from human and rat livers.

AB - 1. 1. Bile acid CoA:amino acid:N-acyltransferase (BAT) was partially purified from dog, human, pig and rat livers. The interspecies variation in substrate specificity and kinetics were determined for glycine and taurine. 2. 2. BAT activity from dog liver formed bile acid conjugates with taurine exclusively, whereas BAT activity from each of the other species formed conjugates with both taurine and glycine. 3. 3. Biliary composition of glycine and taurine bile acid conjugates could partly be accounted for by substrate affinity (Km) and turnover number (Vmax) of BAT activity. 4. 4. A monospecific anti-human BAT polyclonal antibody reacted on Western blot analysis with a 40 kDa band in a 100,000 g supernatant fraction from rat liver. 5. 5. Immunoabsorption chromatography using an anti-human BAT antibody-Sepharose affinity column showed that both the immunoreactive protein band and BAT activity were removed from the 100,000 g supernatant fraction from human and rat livers.

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