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 journalArticle

70 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 (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).

Original languageEnglish
Pages (from-to)97-100
Number of pages4
JournalFEBS Letters
Volume257
Issue number1
DOIs
Publication statusPublished - Oct 23 1989

Fingerprint

Cholesterol 7-alpha-Hydroxylase
Cloning
Molecular Cloning
Liver Microsomes
Liver
Rats
Nucleotides
Complementary DNA
COS Cells
Clone Cells
Enzymes
Gene Library
Cytochrome P-450 Enzyme System
Open Reading Frames
Organism Cloning
Amino Acids
Antibodies

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression. / Noshiro, Mitsuhide; Nishimoto, Masazumi; Morohashi, Ken-Ichirou; Okuda, Kyuichiro.

In: FEBS Letters, Vol. 257, No. 1, 23.10.1989, p. 97-100.

Research output: Contribution to journalArticle

Noshiro, Mitsuhide ; Nishimoto, Masazumi ; Morohashi, Ken-Ichirou ; Okuda, Kyuichiro. / Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression. In: FEBS Letters. 1989 ; Vol. 257, No. 1. pp. 97-100.
@article{2f9a100124fa43ac9d40a38ac6c69c1d,
title = "Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression",
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).",
author = "Mitsuhide Noshiro and Masazumi Nishimoto and Ken-Ichirou Morohashi and Kyuichiro Okuda",
year = "1989",
month = "10",
day = "23",
doi = "10.1016/0014-5793(89)81795-8",
language = "English",
volume = "257",
pages = "97--100",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Molecular cloning of cDNA for cholesterol 7α-hydroxylase from rat liver microsomes. Nucleotide sequence and expression

AU - Noshiro, Mitsuhide

AU - Nishimoto, Masazumi

AU - Morohashi, Ken-Ichirou

AU - Okuda, Kyuichiro

PY - 1989/10/23

Y1 - 1989/10/23

N2 - 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).

AB - 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).

UR - http://www.scopus.com/inward/record.url?scp=0024442549&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024442549&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(89)81795-8

DO - 10.1016/0014-5793(89)81795-8

M3 - Article

C2 - 2806567

AN - SCOPUS:0024442549

VL - 257

SP - 97

EP - 100

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -