Lung contains an inhibitor for nicotinatemononucleotide pyrophosphorylase (carboxylating) of NAD biosynthesis

Richard Seither, Olen R. Brown, B. V. Babu

Research output: Contribution to journalArticle

Abstract

Rat, cow and foal lung extracts contained an inhibitor for the liver NAD biosynthetic-pathway enzyme, nicotinatemononucleotide pyrophosphoryase (carboxylating) [EC 2.4.2.19]. The inhibitor was not dialyzable, was labile at 100°C, was retained by a 30, 000 dalton pore size Amicon membrane and, when partially purified by precipitation at 40-100% ammonium sulfate, inhibited the enzyme stoichiometrically. Lung reportedly does not contain nicotinatemononucleotide pyrophosphorylase or make NAD de novo. However, the inhibitor would mask detection of the enzyme in lung extracts. We detected a low nicotinatemononucleotide pyrophosphorylase-like activity (0.003 ± 0.001 nanomoles CO2 produced from quinolinic acid per mg of extract protein) in rat lung but none in foal or cow lung.

Original languageEnglish (US)
Pages (from-to)253-259
Number of pages7
JournalLife Sciences
Volume48
Issue number3
DOIs
StatePublished - 1991
Externally publishedYes

Fingerprint

Biosynthesis
NAD
Lung
Rats
Enzymes
Quinolinic Acid
Ammonium Sulfate
Liver
Pore size
Masks
Biosynthetic Pathways
Membranes
nicotinate-nucleotide diphosphorylase (carboxylating)
Proteins

ASJC Scopus subject areas

  • Pharmacology

Cite this

Lung contains an inhibitor for nicotinatemononucleotide pyrophosphorylase (carboxylating) of NAD biosynthesis. / Seither, Richard; Brown, Olen R.; Babu, B. V.

In: Life Sciences, Vol. 48, No. 3, 1991, p. 253-259.

Research output: Contribution to journalArticle

@article{ed0b93a5161e48569daffbc83e21acf0,
title = "Lung contains an inhibitor for nicotinatemononucleotide pyrophosphorylase (carboxylating) of NAD biosynthesis",
abstract = "Rat, cow and foal lung extracts contained an inhibitor for the liver NAD biosynthetic-pathway enzyme, nicotinatemononucleotide pyrophosphoryase (carboxylating) [EC 2.4.2.19]. The inhibitor was not dialyzable, was labile at 100°C, was retained by a 30, 000 dalton pore size Amicon membrane and, when partially purified by precipitation at 40-100{\%} ammonium sulfate, inhibited the enzyme stoichiometrically. Lung reportedly does not contain nicotinatemononucleotide pyrophosphorylase or make NAD de novo. However, the inhibitor would mask detection of the enzyme in lung extracts. We detected a low nicotinatemononucleotide pyrophosphorylase-like activity (0.003 ± 0.001 nanomoles CO2 produced from quinolinic acid per mg of extract protein) in rat lung but none in foal or cow lung.",
author = "Richard Seither and Brown, {Olen R.} and Babu, {B. V.}",
year = "1991",
doi = "10.1016/0024-3205(91)90352-C",
language = "English (US)",
volume = "48",
pages = "253--259",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Lung contains an inhibitor for nicotinatemononucleotide pyrophosphorylase (carboxylating) of NAD biosynthesis

AU - Seither, Richard

AU - Brown, Olen R.

AU - Babu, B. V.

PY - 1991

Y1 - 1991

N2 - Rat, cow and foal lung extracts contained an inhibitor for the liver NAD biosynthetic-pathway enzyme, nicotinatemononucleotide pyrophosphoryase (carboxylating) [EC 2.4.2.19]. The inhibitor was not dialyzable, was labile at 100°C, was retained by a 30, 000 dalton pore size Amicon membrane and, when partially purified by precipitation at 40-100% ammonium sulfate, inhibited the enzyme stoichiometrically. Lung reportedly does not contain nicotinatemononucleotide pyrophosphorylase or make NAD de novo. However, the inhibitor would mask detection of the enzyme in lung extracts. We detected a low nicotinatemononucleotide pyrophosphorylase-like activity (0.003 ± 0.001 nanomoles CO2 produced from quinolinic acid per mg of extract protein) in rat lung but none in foal or cow lung.

AB - Rat, cow and foal lung extracts contained an inhibitor for the liver NAD biosynthetic-pathway enzyme, nicotinatemononucleotide pyrophosphoryase (carboxylating) [EC 2.4.2.19]. The inhibitor was not dialyzable, was labile at 100°C, was retained by a 30, 000 dalton pore size Amicon membrane and, when partially purified by precipitation at 40-100% ammonium sulfate, inhibited the enzyme stoichiometrically. Lung reportedly does not contain nicotinatemononucleotide pyrophosphorylase or make NAD de novo. However, the inhibitor would mask detection of the enzyme in lung extracts. We detected a low nicotinatemononucleotide pyrophosphorylase-like activity (0.003 ± 0.001 nanomoles CO2 produced from quinolinic acid per mg of extract protein) in rat lung but none in foal or cow lung.

UR - http://www.scopus.com/inward/record.url?scp=0025965569&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025965569&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(91)90352-C

DO - 10.1016/0024-3205(91)90352-C

M3 - Article

C2 - 1992282

AN - SCOPUS:0025965569

VL - 48

SP - 253

EP - 259

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 3

ER -