| Autor: |
Dumermuth, Eric, Eldering, Joyce A., Grünberg, Jürgen, Jiang, Weiping, Sterchi, Erwin E. |
| Zdroj: |
FEBS Letters; December 1993, Vol. 335 Issue: 3 p367-375, 9p |
| Abstrakt: |
PABA peptide hydrolase (PPH) from human enterocytes is comprised of two submits, alpha and beta. PPHα is over 70% identical to meprin, a protease isolated from mouse and rat kidney. The enzyme shows a modular organization in that it contains an astacin protease domain, an adhesive domain, an EGF‐like domain, and a putative C‐terminal membrane spanning domain. Expression of a chimeric meprin‐PPHα cDNA in COS‐1 cells led to the synthesis of immature, transport‐incompetent homodimers. In addition, complex glycosylated forms were detected in the culture medium, suggesting that the enzyme is secreted after proteolytic removal of the membrane anchor. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Plný text