A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a ‘High‐Km,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism

Elizabeth M. Algar; John L. VandeBerg; Roger S. Holmes

doi:10.1111/j.1530-0277.1992.tb01894.x

A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a ‘High‐K_m,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism

Elizabeth M. Algar, John L. VandeBerg, Roger S. Holmes

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

9 Scopus citations

Abstract

The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using K_cat/K_m, values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed ‘high‐K_m’ properties with respect to ethanol, and is expected to significantly contribute to ‘first‐pass’ metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver ‘low‐K_m’ ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.

Original language	English (US)
Pages (from-to)	922-927
Number of pages	6
Journal	Alcoholism: Clinical and Experimental Research
Volume	16
Issue number	5
DOIs	https://doi.org/10.1111/j.1530-0277.1992.tb01894.x
State	Published - Oct 1992

Keywords

Alcohol Dehydrogenase
Baboon
Ethanol
Stomach

ASJC Scopus subject areas

Medicine (miscellaneous)
Toxicology
Psychiatry and Mental health

Access to Document

10.1111/j.1530-0277.1992.tb01894.x

Fingerprint Dive into the research topics of 'A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a ‘High‐K<sub>m</sub>,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism'. Together they form a unique fingerprint.

Cite this

A Gastric Alcohol Dehydrogenase in the Baboon : Purification and Properties of a ‘High‐K_m,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism. / Algar, Elizabeth M.; VandeBerg, John L.; Holmes, Roger S.

In: Alcoholism: Clinical and Experimental Research, Vol. 16, No. 5, 10.1992, p. 922-927.

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

@article{baa5fb73f91e4741980721f665af3bfd,

title = "A Gastric Alcohol Dehydrogenase in the Baboon: Purification and Properties of a {\textquoteleft}High‐Km,{\textquoteright} Enzyme, Consistent with a Role in {\textquoteleft}First Pass{\textquoteright} Alcohol Metabolism",

abstract = "The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using Kcat/Km, values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed {\textquoteleft}high‐Km{\textquoteright} properties with respect to ethanol, and is expected to significantly contribute to {\textquoteleft}first‐pass{\textquoteright} metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver {\textquoteleft}low‐Km{\textquoteright} ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.",

keywords = "Alcohol Dehydrogenase, Baboon, Ethanol, Stomach",

author = "Algar, {Elizabeth M.} and VandeBerg, {John L.} and Holmes, {Roger S.}",

year = "1992",

month = oct,

doi = "10.1111/j.1530-0277.1992.tb01894.x",

language = "English (US)",

volume = "16",

pages = "922--927",

journal = "Alcoholism: Clinical and Experimental Research",

issn = "0145-6008",

publisher = "Wiley-Blackwell",

number = "5",

}

TY - JOUR

T1 - A Gastric Alcohol Dehydrogenase in the Baboon

T2 - Purification and Properties of a ‘High‐Km,’ Enzyme, Consistent with a Role in ‘First Pass’ Alcohol Metabolism

AU - Algar, Elizabeth M.

AU - VandeBerg, John L.

AU - Holmes, Roger S.

PY - 1992/10

Y1 - 1992/10

N2 - The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using Kcat/Km, values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed ‘high‐Km’ properties with respect to ethanol, and is expected to significantly contribute to ‘first‐pass’ metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver ‘low‐Km’ ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.

AB - The major isozyme of alcohol dehydrogenase in baboon stomach, ADH3, has been purified to homogeneity and characterized with a range of alcohol and aldehyde substrates. Using Kcat/Km, values as an indication of substrate efficacy, medium‐chain length aliphatic alcohols and aldehydes were identified as the preferred substrates. ADH3 showed ‘high‐Km’ properties with respect to ethanol, and is expected to significantly contribute to ‘first‐pass’ metabolism of alcohol. The enzyme exhibited more than two orders of magnitude higher turnover of substrate than the baboon liver ‘low‐Km’ ADH, and may play a role in the rapid metabolism of a wide range of ingested alcohols in the diet.

KW - Alcohol Dehydrogenase

KW - Baboon

KW - Ethanol

KW - Stomach

UR - http://www.scopus.com/inward/record.url?scp=0026794178&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026794178&partnerID=8YFLogxK

U2 - 10.1111/j.1530-0277.1992.tb01894.x

DO - 10.1111/j.1530-0277.1992.tb01894.x

M3 - Article

C2 - 1443431

AN - SCOPUS:0026794178

VL - 16

SP - 922

EP - 927

JO - Alcoholism: Clinical and Experimental Research

JF - Alcoholism: Clinical and Experimental Research

SN - 0145-6008

IS - 5

ER -