| Autor: |
Kuks, P F, Créminon, C, Leseney, A M, Bourdais, J, Morel, A, Cohen, P |
| Zdroj: |
Journal of Biological Chemistry; September 1989, Vol. 264 Issue: 25 p14609-14612, 4p |
| Abstrakt: |
Comparison of the precursor sequence for several peptide hormones of Xenopus laevisskin revealed a consensus sequence around a single arginine cleavage site which is 100% conserved on four residues Arg-Xaa-Val-Arg-Gly (RXVRG). A tetradecapeptide substrate (Asp-Val-Asp-Glu-Arg-Asp-Val-Arg-Gly-Phe-Ala-Ser-Phe-Leu-NH2) was used as a probe to purify and characterize the putative processing endoprotease. A hydrophobic enzyme was purified at least 9000-fold from Xenopusskin exudate by a four-step procedure. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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