Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular identity and cellular localization.

@article{Song1994RatKG,
  title={Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular identity and cellular localization.},
  author={Li Song and Minghao Ye and M Troyanovskaya and Elizabeth Wilk and Sherwin Wilk and Dennis Healy},
  journal={The American journal of physiology},
  year={1994},
  volume={267 4 Pt 2},
  pages={F546-57}
}
Glutamyl aminopeptidase [aminopeptidase A (EAP), EC 3.4.11.7] is an ectoenzyme that selectively hydrolyzes acidic amino acid residues from the amino terminus of oligopeptides. EAP activity is highest within the kidney and small intestine. The murine pre-B cell BP-1/6C3 and the human kidney glycoprotein gp160 differentiation antigens have been reported to have biochemical properties indistinguishable from EAP. It is not known, however, if rat kidney EAP is a homologue of these antigens or… CONTINUE READING