The lactating mammary glands of rats contain an arylhydroxamic acid N,O-acyltransferase that catalyzes the formation of arylamine-substituted nucleic acid on incubation with N-hydroxy-N-2-acetylaminofluorene or N-hydroxy-N-4-acetylaminobiphenyl and transfer RNA. The acyltransferase activity migrates as a single component with a molecular weight of 28,000 on gel filtration on Sephadex G-100.
Acyltransferase activities of the lactating mammary glands of Sprague-Dawley animals are approximately twice those of the less susceptible Fischer strain as determined by assay with either hydroxamic acid. The fluorene substrate was 15 times as efficient as the biphenyl compound in promoting adduct formation.
Ribosomal RNA adducts formed in vivo after administration of N-hydroxy-N-2-acetylaminofluorene were consistent with an acyltransferase mechanism of activation in that the adducts did not retain the acetyl group.
These studies were supported by a grant from the Jules J. Reingold Trust, USPHS Grants CA 13179 from the National Cancer Institute, and CA 15640 from the National Cancer Institute through the National Bladder Cancer Project and the Medical Research Institute Council of Michael Reese Hospital and Medical Center. A preliminary report of these studies was presented at the 1976 meeting of the American Association for Cancer Research (16).