Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid ω-hydroxylase and the cognate enzyme expressed in Escherichia coli

Colin N.A. Palmer, Toby H. Richardson, Keith J. Griffin, Mei Hui Hsu, A. Scott Muerhoff, Joan E. Clark, Eric F. Johnson (Lead / Corresponding author)

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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 languageEnglish
Pages (from-to)161-166
Number of pages6
JournalBBA - Gene Structure and Expression
Volume1172
Issue number1-2
DOIs
Publication statusPublished - 20 Feb 1993

Keywords

  • (Human kidney)
  • Arachidonic acid
  • CYP4AII
  • Cytochrome P-450
  • Fatty acid
  • ω-Hydroxylase

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