N-Nitrosobutyl(4-hydroxybutyl)amine alpha-hydroxylation by rat liver and urothelial cell homogenates.

L. Airoldi, C. Magagnotti, M. Bonfanti, M. Moret, R. Fanelli

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Determination of molecular nitrogen formed as a consequence of nitrosamine alpha-hydroxylation provides a useful means for studying the extent of activation of these compounds in target and nontarget organs and tissues. alpha-Hydroxylation in rat liver and urothelial cells was compared using as substrate doubly 15N-labelled N-nitrosobutyl(4-hydroxybutyl)amine (15N-NBHBA), a potent bladder carcinogen in rodents. Both enzyme sources metabolized 15N-NBHBA through the alpha-hydroxylation pathway. 15N2 production was dependent on the amount of substrate incubated. Vmax values for 15N2 production by urothelial cells and by liver postmitochondrial supernatant were 4.47 and 3.21 nmol/mg protein per h, respectively.

Original languageEnglish
Pages (from-to)343-345
Number of pages3
JournalIARC scientific publications
Issue number105
Publication statusPublished - 1991

Fingerprint

Hydroxylation
Amines
Liver
Nitrosamines
Carcinogens
Rodentia
Urinary Bladder
Nitrogen
Enzymes
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

N-Nitrosobutyl(4-hydroxybutyl)amine alpha-hydroxylation by rat liver and urothelial cell homogenates. / Airoldi, L.; Magagnotti, C.; Bonfanti, M.; Moret, M.; Fanelli, R.

In: IARC scientific publications, No. 105, 1991, p. 343-345.

Research output: Contribution to journalArticle

@article{85367e2f7a464e1ab24831700f45c339,
title = "N-Nitrosobutyl(4-hydroxybutyl)amine alpha-hydroxylation by rat liver and urothelial cell homogenates.",
abstract = "Determination of molecular nitrogen formed as a consequence of nitrosamine alpha-hydroxylation provides a useful means for studying the extent of activation of these compounds in target and nontarget organs and tissues. alpha-Hydroxylation in rat liver and urothelial cells was compared using as substrate doubly 15N-labelled N-nitrosobutyl(4-hydroxybutyl)amine (15N-NBHBA), a potent bladder carcinogen in rodents. Both enzyme sources metabolized 15N-NBHBA through the alpha-hydroxylation pathway. 15N2 production was dependent on the amount of substrate incubated. Vmax values for 15N2 production by urothelial cells and by liver postmitochondrial supernatant were 4.47 and 3.21 nmol/mg protein per h, respectively.",
author = "L. Airoldi and C. Magagnotti and M. Bonfanti and M. Moret and R. Fanelli",
year = "1991",
language = "English",
pages = "343--345",
journal = "IARC (International Agency for Research on Cancer) Scientific Publications",
issn = "0300-5038",
publisher = "IARC",
number = "105",

}

TY - JOUR

T1 - N-Nitrosobutyl(4-hydroxybutyl)amine alpha-hydroxylation by rat liver and urothelial cell homogenates.

AU - Airoldi, L.

AU - Magagnotti, C.

AU - Bonfanti, M.

AU - Moret, M.

AU - Fanelli, R.

PY - 1991

Y1 - 1991

N2 - Determination of molecular nitrogen formed as a consequence of nitrosamine alpha-hydroxylation provides a useful means for studying the extent of activation of these compounds in target and nontarget organs and tissues. alpha-Hydroxylation in rat liver and urothelial cells was compared using as substrate doubly 15N-labelled N-nitrosobutyl(4-hydroxybutyl)amine (15N-NBHBA), a potent bladder carcinogen in rodents. Both enzyme sources metabolized 15N-NBHBA through the alpha-hydroxylation pathway. 15N2 production was dependent on the amount of substrate incubated. Vmax values for 15N2 production by urothelial cells and by liver postmitochondrial supernatant were 4.47 and 3.21 nmol/mg protein per h, respectively.

AB - Determination of molecular nitrogen formed as a consequence of nitrosamine alpha-hydroxylation provides a useful means for studying the extent of activation of these compounds in target and nontarget organs and tissues. alpha-Hydroxylation in rat liver and urothelial cells was compared using as substrate doubly 15N-labelled N-nitrosobutyl(4-hydroxybutyl)amine (15N-NBHBA), a potent bladder carcinogen in rodents. Both enzyme sources metabolized 15N-NBHBA through the alpha-hydroxylation pathway. 15N2 production was dependent on the amount of substrate incubated. Vmax values for 15N2 production by urothelial cells and by liver postmitochondrial supernatant were 4.47 and 3.21 nmol/mg protein per h, respectively.

UR - http://www.scopus.com/inward/record.url?scp=0026066868&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026066868&partnerID=8YFLogxK

M3 - Article

C2 - 1855877

AN - SCOPUS:0026066868

SP - 343

EP - 345

JO - IARC (International Agency for Research on Cancer) Scientific Publications

JF - IARC (International Agency for Research on Cancer) Scientific Publications

SN - 0300-5038

IS - 105

ER -