Isolation of a full-length cDNA encoding mouse aromatase P450

A full-length cDNA clone for aromatase P450 has been isolated from a pregnant mouse ovarian cDNA library. The insert of this clone (2394 bp) contains a 1509-bp open reading frame encoding 503 amino acid residues together with a 46-bp 5′-untranslated stretch and an 839-bp 3′-untranslated region to wh...

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Veröffentlicht in:Archives of biochemistry and biophysics 1991-03, Vol.285 (2), p.231-237
Hauptverfasser: Terashima, Masako, Toda, Katsumi, Kawamoto, Takeshi, Kuribayashi, Isao, Ogawa, Yasuhiro, Maeda, Tomoho, Shizuta, Yutaka
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Sprache:eng
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Zusammenfassung:A full-length cDNA clone for aromatase P450 has been isolated from a pregnant mouse ovarian cDNA library. The insert of this clone (2394 bp) contains a 1509-bp open reading frame encoding 503 amino acid residues together with a 46-bp 5′-untranslated stretch and an 839-bp 3′-untranslated region to which a poly(A) tract is attached. Northern blot analysis of ovarian RNA from pregnant mice reveals a major mRNA band of 2.5 kb with a minor band of 2.1 kb. Comparison of mouse aromatase P450 with that of rat, human, and chicken shows 91, 81, and 69% identity in the nucleotide sequence and 92, 79, and 69% identity in the deduced amino acid sequence, respectively. The membrane-spanning domain of mouse aromatase P450 is estimated to be an extremely hydrophobic segment located within the N-terminal region of the molecule. Furthermore, a highly conserved heme-binding domain is noticed.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(91)90354-L