@article {Seralini_etal2003,
	title = {{Molecular characterization and expression of equine testicular cytochrome P450 aromatase*1}},
	journal = {Biochimica et Biophysica Acta (BBA) {\textendash} Gene Structure and Expression},
	volume = {1625},
	number = {3},
	year = {2003},
	pages = {229{\textendash}238},
	abstract = {We characterized testicular equine aromatase and its expression. A 2707 bp cDNA was isolated, it encoded a polypeptide of 503 residues with a deduced molecular mass of 57.8 kDa. The sequence features were those of a cytochrome P450 aromatase, with a 78\% polypeptide identity with the human counterpart. The gene has a minimal length of 74 kb comprising at least 9 exons and expresses a 2.8 kb mRNA in the testis. Transient cDNA transfections in E293 cells and in vitro translations in a reticulocyte lysate system allowed aromatase protein and activity detections. The activity increased with androstenedione as substrate in a dose-dependent manner. The isolation of testicular aromatase by a new immunoaffinity method demonstrated that the protein could exist either glycosylated or not with a 2 kDa difference. All these results taken together allow new structural studies to progress in the understanding of this cytochrome P450.},
	author = {Seralini, G-E and Tomilin, A and Auvray, P and Nativelle-Serpentini, C and Pascal Sourdaine and Moslemi, S}
}
