Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A

M. Vilanova, J. Vendrell, C. M. Cuchillo, F. X. Aviles

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

The isolated activation segment of pig procarboxypeptidase A binds two Tb3+ ions in a strong and specific way. In contrast, the binding of Ca2+, Cd2+ and Mg2+ is weak. The binding of Tb3+ increases the resistance of the isolated activation segment against proteolysis and competes for the binding of the carbocyanine dye Stains-A11. This dye forms complexes with the activation segment showing spectral properties similar to those observed with EF-hand structures. The presented results support a previous hypothesis on the existence of two regions in the activation segment of pancreatic procarboxypeptidases structurally related to Ca2+-binding domains of the EF-hand protein family.
Original languageEnglish
Pages (from-to)901-905
JournalBiochemical Journal
Volume251
Issue number3
DOIs
Publication statusPublished - 1 Jan 1988

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