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 language||English (US)|
|Number of pages||4|
|Journal||Biochimica et Biophysica Acta - Gene Structure and Expression|
|State||Published - Oct 1997|
- Aminopeptidase P
ASJC Scopus subject areas
- Structural Biology