Detail of "92-67-1"

Reference

In vivo dosimetry of 4-aminobiphenyl in rats via a cysteine adduct in hemoglobin

In vivo dosimetry of 4-aminobiphenyl in rats via a cysteine adduct in hemoglobin. Green, Laura C.; Skipper, Paul L.; Turesky, Robert J.; Bryant, Matthew S.; Tannenbaum, Steven R. (Dep. Nutr. Food Sci., Massachusetts Inst. Technol., Cambridge, MA 02139, USA). Cancer Res., 44(10), 4254-9 (English) 1984. CODEN: CNREA8. ISSN: 0008-5472. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) The feasibility of monitoring doses of 4-aminobiphenyl (ABP)(I) [92-67-1] via adduction to Hb was investigated. Rats dosed with ABP (from 0.5 mg/kg to 5 mg/kg) formed a stable covalent Hb:ABP adduct. Approx. 5% of a single dose was bound as Hb:ABP; chronic dosing led to an accumulation of the adduct to a level 30 times greater than that found after a single dose. Facile in vitro hydrolysis of the adduct regenerated ABP, allowing detection at the subnanogram level. Human Hb was also readily adducted, using N-hydroxy-ABP [6810-26-0] in vitro. The predominant site of adduction appeared to be the cysteine residue in Hb. The use of such adducts as dosimeters for arylamine exposures in humans is discussed.

Metabolic activation of carcinogenic aromatic amines by dog bladder and kidney prostaglandin H synthase

Metabolic activation of carcinogenic aromatic amines by dog bladder and kidney prostaglandin H synthase. Wise, Ronald W.; Zenser, Terry V.; Kadlubar, Fred F.; Davis, Bernard B. (Clin. Cent., Veterans Adm. Med. Cent., St. Louis, MO 63125, USA). Cancer Res., 44(5), 1893-7 (English) 1984. CODEN: CNREA8. ISSN: 0008-5472. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Microsomal enzyme prepns. from dog liver, kidney, and bladder were used to assess the prostaglandin H synthase [59763-19-8]-catalyzed activation of carcinogenic arom. amines to bind covalently to proteins and nucleic acids. Benzidine [92-87-5], a urinary bladder carcinogen, bound to protein of bladder transitional epithelial and renal inner and outer medullary microsomes and was dependent upon addn. of arachidonic acid, but not upon reduced NADHP. Bladder transitional epithelial microsomes also activated o-dianisidine [119-90-4], 4-aminobiphenyl [92-67-1], and 2-naphthylamine [91-59-8] to bind to protein and tRNA and benzidine and o-dianisidine to bind DNA. Cosubstrate and inhibitor specificities were consistent with activation by prostaglandin H synthase. Binding of benzidine to protein was not obsd. with either hepatic or renal cortical microsomes upon addn. of arachidonic acid or NADHP. Prostaglandin H synthase and mixed-function oxidase [9040-60-2]-catalyzed bindings of 2-naphthylamine to protein and to tRNA were compared using liver and bladder microsomes. Only mixed-function oxidase-catalyzed binding was obsd. in liver, and only prostaglandin H synthase-catalyzed binding was obsd. in bladder. The rate of binding catalyzed by bladder microsomes was considerably greater than that catalyzed by hepatic microsomes. In addn., the bladder content of prostaglandin H synthase activity was approx. 10 times that of kidney inner medullary, a tissue reported to have a relatively high content of this enzyme in other species. These results are consistent with involvement of bladder transitional epithelial prostaglandin H synthase in the genesis of primary arom. amine-induced bladder cancer.