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

doi:10.1016/0305-0491(91)90095-U

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

Pharmacology

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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 (K_m) and turnover number (V_max) 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 language	English (US)
Pages (from-to)	131-136
Number of pages	6
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	100
Issue number	1
DOIs	https://doi.org/10.1016/0305-0491(91)90095-U
State	Published - 1991

ASJC Scopus subject areas

Biochemistry
Physiology
Molecular Biology

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

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.",

author = "Kwakye, {Joseph B.} and Johnson, {Martin R.} and Stephen Barnes and Diasio, {Robert B.}",

year = "1991",

doi = "10.1016/0305-0491(91)90095-U",

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T1 - A comparative study of bile acid CoA:Amino acid:N-acyltransferase (BAT) from four mammalian species

AU - Kwakye, Joseph B.

AU - Johnson, Martin R.

AU - Barnes, Stephen

AU - Diasio, Robert B.

PY - 1991

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

Abstract

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