Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression

Mitsuhide Noshiro; Masazumi Nishimoto; Ken ichirou Morohashi; Kyuichiro Okuda

doi:10.1016/0014-5793(89)81795-8

Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression

Mitsuhide Noshiro, Masazumi Nishimoto, Ken ichirou Morohashi, Kyuichiro Okuda

Research output: Contribution to journal › Article › peer-review

90 Citations (Scopus)

Abstract

A complete cDNA clone encoding cholesterol 7α-hydroxylase was isolated from a rat liver cDNA library by the use of specific antibodies to the enzyme. The isolated cDNA clone was 3.6 kbp long and contained a 1509-bp open reading frame encoding 503 amino acid residues (M_r = 56 880). The identity of the cDNA was confirmed by expression of cholesterol 7α-hydroxylase activity and the immunoreactive protein in COS cells transfected with pSVL expression vector carrying the cDNA insert. The primary structure of cholesterol 7α-hydroxylase deduced from the nucleotide sequence of the cDNA indicated that the enzyme constitutes a novel P-450 family. Cholesterol 7α-hydroxylase; Cytochrome P-450; cDNA cloning; (COS cell).

Original language	English
Pages (from-to)	97-100
Number of pages	4
Journal	FEBS Letters
Volume	257
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(89)81795-8
Publication status	Published - Oct 23 1989
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(89)81795-8

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abstract = "A complete cDNA clone encoding cholesterol 7α-hydroxylase was isolated from a rat liver cDNA library by the use of specific antibodies to the enzyme. The isolated cDNA clone was 3.6 kbp long and contained a 1509-bp open reading frame encoding 503 amino acid residues (Mr = 56 880). The identity of the cDNA was confirmed by expression of cholesterol 7α-hydroxylase activity and the immunoreactive protein in COS cells transfected with pSVL expression vector carrying the cDNA insert. The primary structure of cholesterol 7α-hydroxylase deduced from the nucleotide sequence of the cDNA indicated that the enzyme constitutes a novel P-450 family. Cholesterol 7α-hydroxylase; Cytochrome P-450; cDNA cloning; (COS cell).",

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AU - Noshiro, Mitsuhide

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AU - Morohashi, Ken ichirou

AU - Okuda, Kyuichiro

PY - 1989/10/23

Y1 - 1989/10/23

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Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression

Abstract

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