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Science 20 January 1978:
Vol. 199. no. 4326, pp. 307 - 309
DOI: 10.1126/science.619459
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Articles

Science, Vol 199, Issue 4326, 307-309
Copyright © 1978 by American Association for the Advancement of Science

articles

beta-Glucuronidase catalyzed hydrolysis of benzo(a)pyrene-3-glucuronide and binding to DNA

N Kinoshita and HV Gelboin

beta-Glucuronidase catalyzes the hydrolysis of benzo[a]pyrene-3-glucuronide to 3-hydroxybenzo[a]pyrene. During the enzymatic hydrolysis, a benzo[a]pyrene derivative is formed which binds to DNA to a far greater extent than either the 3-hydroxybenzo[a]pyrene or its glucuronide. These results suggest that conjugates of benzo(a)pyrene may be converted by beta-glucuronidase at intracellular and organ sites distal to the initial sites of oxygenation and conjugation of benzo(a)pyrene to activated intermediates that are possibly carcinogenic.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Intestinal Bioavailability and Biotransformation of 3-Hydroxybenzo(a)pyrene in an Isolated Perfused Preparation from Channel Catfish, Ictalurus punctatus.
M. O. James, Z. Tong, L. Rowland-Faux, C. S. Venugopal, and K. M. Kleinow (2001)
Drug Metab. Dispos. 29, 721-728
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