期刊论文详细信息
FEBS Letters
Expression of cytochrome P‐450d by Saccharomyces cerevisiae
Fujii-Kuriyama, Yoshiaki1  Ogoma, Yoshiro1  Hatano, Masahiro1  Takahashi, Masae1  Sogawa, Kazuhiro1  Shimizu, Toru1 
[1] Chemical Research Institute of Non-Aqueous Solutions, Tohoku University, Sendai 980, Japan
关键词: Cytochrome P-450;    (Yeast);    Expression;    cDNA;    P-450;    cytochrome P-450;    P-450d;    cytochrome P-450d;    17β-estradiol;    estra-1;    3;    5(10)-triene-3;    17β-diol;    isosafrole;    5-(1-propenyl)-1;    3-benzodioxole;    phenobarbital;    5-ethyl-5-phenyl-2;    4;    6(1H;    3H;    5H)-pyrimidinetrione;    3-methylcholanthrene;    1;    2-dihydro-3-methylbenz(j)aceanthrylene;    ampicillin;    6-[D-(2-amino-2-phenylacetoamido)]-3;    3-dimethyl-7-oxo-4-thia-1-azabicyclo(3;    2;    0)heptane-2-carboxylic acid;   
DOI  :  10.1016/0014-5793(86)81491-0
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Rat liver microsomal cytochrome P-450d was abundantly expressed in the yeast Saccharomyces cerevisiae by using a yeast-Escherichia coli shuttle vector consisting of rat liver P-450d cDNA and yeast acid phosphatase promoter. The expressed cytochrome P-450d was immunologically crossed with rat liver P-450d. The hydroxylase activity of estra-1,3,5(10)-triene-3,17β-diol was 11 nmol/min per nmol P-450d, which is comparable to that reported previously for rat liver P-450d. The expressed P-450d content was nearly 1% of total yeast protein as estimated from immunoblotting, hydroxylase activity and optical absorption of the reduced CO form.

【 授权许可】

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