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Reaction kinetics of the aromatase enzyme and of a new nonsteroidal aromatase inhibitor, R 76 713 (6-[(4-chlorophenyl)(1H-1,2,4-triazol-1-yl)-methyl]-1-methyl-1H- benzotriazole), were studied in ovarian homogenates obtained from pregnant mare's serum gonadotropin (PMSG)-injected female Wistar rats. The Km (Michaelis constant) of the aromatase enzyme with androstenedione as the substrate was 47 +/- 13 nM; for testosterone as the substrate, a value of 159 +/- 10 nM was found. In the presence of increasing concentrations of R 76 713, the Km increased while the Vmax (maximal velocity of enzyme-catalyzed reaction) remained unchanged. Using androstenedione and testosterone as the substrate, Lineweaver-Burk analysis of the data showed a Ki (dissociation constant of the enzyme-inhibitor complex) for R 76 713 of 0.7 +/- 0.3 nM and 1.6 +/- 0.4 nM, respectively. R 76 713 appeared to competitively inhibit the rat ovarian aromatase.
M D Krekels, and
W Wouters, and
R De Coster
November 1986,
Research communications in chemical pathology and pharmacology,
M D Krekels, and
W Wouters, and
R De Coster
September 1983,
Biology of reproduction,
M D Krekels, and
W Wouters, and
R De Coster
January 1989,
Journal of steroid biochemistry,
M D Krekels, and
W Wouters, and
R De Coster
March 1955,
Canadian journal of biochemistry and physiology,
M D Krekels, and
W Wouters, and
R De Coster
June 2014,
Obesity (Silver Spring, Md.),
M D Krekels, and
W Wouters, and
R De Coster
May 1957,
Biochimica et biophysica acta,
M D Krekels, and
W Wouters, and
R De Coster
February 1958,
The Biochemical journal,
M D Krekels, and
W Wouters, and
R De Coster
August 1986,
Experimental and clinical endocrinology,
M D Krekels, and
W Wouters, and
R De Coster
October 1966,
The Journal of biological chemistry,
M D Krekels, and
W Wouters, and
R De Coster
March 1994,
The Journal of endocrinology,
