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Division of Cancer Research, Department of Medicine, Michael Reese Medical Center [C. M. K., C. W. O.], and the University of Chicago Pritzker School of Medicine [C. M. K.], Chicago, Illinois 60616
The activity of arylhydroxamic acid acyltransferase, an enzyme that promotes the introduction of arylamine groups into nucleic acids, is greater in the stomach, small intestine, colon, and lung of the Sprague-Dawley rat than in comparable tissues of Fischer animals. The enzyme is distributed relatively evenly from the glandular stomach to the distal portion of the colon. No consistent differences in acyltransferase activities of the liver, kidney, brain, or spleen of these two strains were noted.
Acyltransferase activity was readily demonstrable in the livers of guinea pigs, hamsters, rabbits, and monkeys; in the kidneys of guinea pigs and hamsters; in the stomachs of guinea pigs and hamsters; in the small intestines of guinea pigs, hamsters, rabbits, and monkeys; in the colons of guinea pigs and hamsters; and in lungs of hamsters. Mouse, dog, and goat tissues were essentially devoid of acyltransferase activity.
The transformation of N-hydroxy-N-2-fluorenylacetamide into a reactive species by conjugation with sulfate was carried out with 105,000 x g supernatants of liver from Sprague-Dawley and Fischer rats and their F1 hybrids. The abilities of liver extracts from the hybrids to carry out this activation were intermediate between those from animals of the same sex of the two parental strains.
1 These studies were supported by a grant from the Jules J. Reingold Trust, NIH Research Grants CA 13179 and 15640 from the National Cancer Institute, and the Medical Research Institute Council of Michael Reese Medical Center. Presented in part at the 64th Annual Meeting of the American Association for Cancer Research, Atlantic City, N. J., April 12, 1973 (13).
Received 9/ 9/74. Accepted 12/16/74.
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