Biochem Biophys Res Commun. 1986 Mar 28;135(3):713-9.

Amino terminal sequence analysis of human placenta aromatase.

Chen S, Shively JE, Nakajin S, Shinoda M, Hall PF.

Abstract

The amino acid composition and the amino-terminal amino acid sequence from position 1 to 21 of human placenta aromatase were determined. In addition, a cysteine containing peptide with a sequence homologous to those of peptides containing the cysteine residue which was suggested to provide the proximal thiolate ligand to the heme in other cytochrome p-450 isozymes, was identified. The results indicate that aromatase is a cytochrome p-450 protein, probably derived from a new cytochrome p-450 family.

PMID:: 3964273; [PubMed - indexed for MEDLINE]

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Purification and characterization of aromatase from human placenta. [Steroids. 1987]
Purification and characterization of aromatase from human placenta.
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Cited by 2 PubMed Central articles

Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA. [Proc Natl Acad Sci U S A. 1986]
Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA.
Evans CT, Ledesma DB, Schulz TZ, Simpson ER, Mendelson CR. Proc Natl Acad Sci U S A. 1986 Sep; 83(17):6387-91.
Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells. [Proc Natl Acad Sci U S A. 1988]
Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells.
Corbin CJ, Graham-Lorence S, McPhaul M, Mason JI, Mendelson CR, Simpson ER. Proc Natl Acad Sci U S A. 1988 Dec; 85(23):8948-52.

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