Abstract
A cDNA encoding a cytochrome P-450 4A (CYP4AII) was cloned from a human kidney cDNA library. Northern blot analysis and RNase protection assays indicate that related mRNAs occur in kidney and liver with the highest abundance found in kidney. The enzyme was expressed from its cDNA in Escherichia coli. A solubilized preparation of the enzyme reconstituted with cytochrome P-450 reductase catalyzed the ω-hydroxylation of lauric acid, palmitic acid, and arachidonic acid with turnover numbers of 9.8, 2.2 and 0.55 min-1, respectively. Little or no activity was detected toward prostaglandins A1 and E1.
Original language | English |
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Pages (from-to) | 161-166 |
Number of pages | 6 |
Journal | BBA - Gene Structure and Expression |
Volume | 1172 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 20 Feb 1993 |
Keywords
- (Human kidney)
- Arachidonic acid
- CYP4AII
- Cytochrome P-450
- Fatty acid
- ω-Hydroxylase
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics