Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2

David Reverter, Isabel García-Sáez, Lluis Catasús, Josep Vendrell, Miquel Coll, Francesc X. Avilés

Research output: Contribution to journalArticleResearchpeer-review

15 Citations (Scopus)

Abstract

Human procarboxypeptidase A2 has been expressed in a Pichia pastoris heterologous system and purified by hydrophobic interaction and anion exchange chromatographies. The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan, was found; with such substrates its activity is similar or higher than that of bovine carboxypeptidase A1. Procarboxypeptidase A2 has been crystallised using a vapour diffusion approach; the crystals obtained belong to the monoclinic system, spacegroup P21, and present one procarboxypeptidase A2 molecule per asymmetric unit. The crystals diffract beyond 1.8 Å resolution and are suitable for detailed X-ray analysis.
Original languageEnglish
Pages (from-to)7-10
JournalFEBS Letters
Volume420
DOIs
Publication statusPublished - 22 Dec 1997

Keywords

  • Carboxypeptidase A2
  • Crystallography
  • Proenzyme
  • Substrate specificity

Fingerprint

Dive into the research topics of 'Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2'. Together they form a unique fingerprint.

Cite this