Cloning and functional expression of the cytoplasmic form of rat aminopeptidase P

Gábor Czirják, William A. Burkhart, Mary B. Moyer, József Antal, Stephen B. Shears, Péter Enyedi

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14 Citations (Scopus)


A rat cytoplasmic aminopeptidase P was purified from liver cytosol with a procedure including an affinity elution step with 3 μM inositol 1,3,4- trisphosphate. Proteolytic fragments were generated, sequenced and the enzyme was cloned from a rat liver cDNA library. The structure shows high (87.8% and 95.5%, respectively) sequence identity at the nucleotide and amino acid levels with the previously described human putative cytoplasmic aminopeptidase P. The cloned rat enzyme was functionally expressed in Escherichia coli and also in COS-1 cells. Western blot analysis, using an antibody generated against the recombinant protein, and Northern blot hybridization showed ubiquitous expression of the protein in different tissues with the highest expression level in the testis.

Original languageEnglish
Pages (from-to)326-336
Number of pages11
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Issue number3
Publication statusPublished - Mar 19 1999


  • Aminopeptidase P
  • Cytoplasmic
  • Functional expression
  • cDNA cloning

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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