Literature DB >> 3856221

N-nitrosodialkylamines do not function as substrates for liver monoamine oxidase.

D E Edmondson, T C Bruice.   

Abstract

Since reports in the literature [Rowland, I.R., Lake, B. G. & Gangolli, S. D. (1980) Mutat. Res. 72, 63-72] have implicated hepatic monoamine oxidase (EC 1.4.3.4) in the activation of N-nitrosodialkylamines to mutagens, it is of basic pharmacological and biochemical interest to determine if these compounds could serve as substrates for this enzyme. The dialkylnitrosamines N-nitrosodiethylamine, N-nitrosodimethylamine, and N-nitrosodibenzylamine were tested and found not to be substrates, competitive inhibitors, or irreversible inhibitors of liver monoamine oxidase. Thus, any role for monoamine oxidase participation in the mutagenic activation of these compounds must be subsequent to an initial conversion of these compounds to their respective secondary amines.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3856221      PMCID: PMC397109          DOI: 10.1073/pnas.82.3.682

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  12 in total

1.  Purification of amine oxidase from beef plasma.

Authors:  C W TABOR; H TABOR; S M ROSENTHAL
Journal:  J Biol Chem       Date:  1954-06       Impact factor: 5.157

2.  The covalently-bound flavin of hepatic monoamine oxidase. 2. Identification and properties of cysteinyl riboflavin.

Authors:  W H Walker; E B Kearney; R L Seng; T P Singer
Journal:  Eur J Biochem       Date:  1971-12

3.  Monoamine oxidase from beef liver mitochondria: simplified isolation procedure, properties, and determination of its cysteinyl flavin content.

Authors:  J I Salach
Journal:  Arch Biochem Biophys       Date:  1979-01       Impact factor: 4.013

4.  Mitochondrial monoamine oxidase. Mechanism of inhibition by phenylhydrazine and by aralkylhydrazines. Role of enzymatic oxidation.

Authors:  D R Patek; L Hellerman
Journal:  J Biol Chem       Date:  1974-04-25       Impact factor: 5.157

5.  Separation and purification of multiple forms of microsomal cytochrome P-450. Activities of different forms of cytochrome P-450 towards several compounds of environmental interest.

Authors:  F P Guengerich
Journal:  J Biol Chem       Date:  1977-06-10       Impact factor: 5.157

6.  Kinetic studies on the catalytic mechanism of liver monoamine oxidase.

Authors:  M Husain; D E Edmondson; T P Singer
Journal:  Biochemistry       Date:  1982-02-02       Impact factor: 3.162

7.  Substrates and inhibitors of hepatic amine oxidase inhibit dimethylnitrosamine-induced mutagenesis in Salmonella typhimurium.

Authors:  I R Rowland; B G Lake; J C Phillips; S D Gangolli
Journal:  Mutat Res       Date:  1980-08       Impact factor: 2.433

8.  Inhibition of monoamine oxidase by N-phenacyl-cyclopropylamine.

Authors:  R W Fuller; S K Hemrick; J Mills
Journal:  Biochem Pharmacol       Date:  1978       Impact factor: 5.858

9.  The role of highly purified forms of rat liver cytochrome P-450 in the dimethylation of dimethylnitrosamine and its activation to mutagens.

Authors:  H A Masson; C Ioannides; G G Gibson
Journal:  Toxicol Lett       Date:  1983-06       Impact factor: 4.372

10.  Metabolic nitrite formation from N-nitrosamines: evidence for a cytochrome P-450 dependent reaction.

Authors:  K E Appel; H Graf
Journal:  Carcinogenesis       Date:  1982       Impact factor: 4.944

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.