The effects of Al(III) speciation on the activity of trypsin

Ágnes Dörnyei, Melinda Kilyén, Tamás Kiss, Béla Gyurcsik, Ilona Laczkó, Attila Pécsváradi, L. Mária Simon, Márta Kotormán

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The effects of the different forms of Al(III) on the catalytic activity of the serine protease trypsin were studied. Enzyme activity was measured by BAEE assay in the presence of AlCl3, Al(III):lactic acid 1:3, Al(III):maltol 1:3 or Al(III):nitrilotriacetic acid (NTA) 1:1 at a nominal Al(III) concentration of 0.01 M, and the ligand alone at pH 7.4 at 25°C. Maltol and NTA caused ∼30% inhibition, while that for the corresponding Al(III) complex was less than half of this. Al(III) in the form of the chloride or in three equivalents of lactic acid did not influence the activity of the enzyme, probably because most of the Al(III) was precipitated as Al(OH) 3. No direct interaction could be detected between the enzyme and the Al(III) complexes, either by ultrafiltration or by CD spectroscopy. These results strongly suggest that there is no direct involvement of Al(III) in the enzymatic reactions of trypsin.

Original languageEnglish
Pages (from-to)118-123
Number of pages6
JournalJournal of Inorganic Biochemistry
Volume97
Issue number1
DOIs
Publication statusPublished - Sep 15 2003

    Fingerprint

Keywords

  • Al(III) complexes
  • CD spectroscopy
  • Enzyme inhibition
  • Serine protease
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this