2. Academic Validation
  3. Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase

Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase

  • FEBS Lett. 1990 Jul 30;268(1):137-40. doi: 10.1016/0014-5793(90)80992-r.
M Noshiro 1,  K Okuda
Affiliations

Affiliation

  • 1 Department of Biochemistry, School of Dentistry, Hiroshima University, Japan.
PMID: 2384150 DOI: 10.1016/0014-5793(90)80992-r
Abstract

A complete cDNA clone encoding human Cholesterol 7 alpha-hydroxylase has been isolated using a rat P-450ch7 alpha cDNA insert [(1989) FEBS Lett. 257, 97-100] as a probe and totally sequenced. The cDNA contained 1512-base pair open reading frame encoding 504 amino acid residues (Mr 57,630), 39-base pair 5'-untranslated region 1322-base pair 3'-ultranslated region including 20 nucleotides of poly A tail in the total length of 2873 base pairs. The deduced amino acid sequence showed 82% similarity to rat P-450ch7 alpha. Unique amino acid residues were observed in putative binding domains for heme and steroid which are highly conserved in most steroidogenic P-450s.

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