Abstract:
:Hepatic microsomes of female F344 rats were capable of N,O-acyltransfer of N-hydroxy-N-acetyl-2-aminofluorene (N-OH-AAF) and N-hydroxy-N-formyl-2-aminofluorene (N-OH-FAF), N-deacetylation of N-OH-AAF and N-acetyl-2-aminofluorene (2-AAF), and O-deacetylation of 4-nitrophenyl acetate (NPA). The activity for N,O-acyltransfer of N-OH-FAF was approximately 20 times greater than that of N-OH-AAF. These microsomal activities were inducible by phenobarbital and were inhibitible by paraoxon. Four distinct N,O-acyltransferases were purified from solubilized hepatic microsomes of phenobarbital pretreated rats. These enzymes were purified to homogeneity, as judged by SDS-PAGE and analytical IEF. Their pIs were approximately 5.0, 5.5, 6.0 and 6.5 and their mol. wts were approximately 60, 61, 180 (a homotrimer of 59 kDa) and 60 kDa respectively. All the enzymes catalyzed the N,O-acyltransfer of N-OH-FAF, the N-deacetylation of N-OH-AAF and 2-AAF and the O-deacetylation of NPA. Among these four enzymes, the hydrolysis of NPA was best catalyzed by pI 6.5 protein, of 2-AAF by the pI 5.5 protein, and of N-OH-AAF by the pI 5.0 protein. The pI 5.5 and pI 6.5 proteins were equally active for N,O-acyltransferase and were more active than the other enzymes. The present study demonstrates that rat hepatic microsomal activities of N,O-acyltransfer, N-deacetylation and O-deacetylation are attributable to the same enzymes.
journal_name
Carcinogenesisjournal_title
Carcinogenesisauthors
Wang CY,Zukowski K,Lee MS,Sone Tdoi
10.1093/carcin/13.11.2017keywords:
subject
Has Abstractpub_date
1992-11-01 00:00:00pages
2017-20issue
11eissn
0143-3334issn
1460-2180journal_volume
13pub_type
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