Cloning and tissue distribution of human membrane-bound aminopeptidase P

Richard C. Venema, Hong Ju, Rong Zou, Virginia J. Venema, James W. Ryan

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


Complementary DNA clones encoding human membrane-bound aminopeptidase P (AMP) were isolated by reverse transcription-polymerase chain reaction (RT- PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83% amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane- bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.

Original languageEnglish (US)
Pages (from-to)45-48
Number of pages4
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Issue number1
StatePublished - Oct 1997


  • Aminopeptidase P
  • Bradykinin

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics


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