Effects of Ca2+ on catalytic activity and conformation of trypsin and α-chymotrypsin in aqueous ethanol

M. Kotormán, I. Laczkó, A. Szabó, L. M. Simon

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The effects of calcium ions on the conformation and catalytic activity of trypsin and α-chymotrypsin were studied in aqueous ethanol. The activity of α-chymotrypsin was practically lost within 10min in the presence of 60% ethanol while trypsin preserved about 40% of its original activity even in 85% ethanol at pH 3. The catalytic activity of α-chymotrypsin did not decrease in the presence of 1.2M CaCl2 and 0.6M CaCl2 with trypsin in ethanolic solvent. In the latter case an activation of enzyme was observed. The stabilizing effects of calcium ions were accompanied by an increase in the helical content in both enzymes, as followed by circular dichroism measurements.

Original languageEnglish
Pages (from-to)18-21
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume304
Issue number1
DOIs
Publication statusPublished - Apr 25 2003

Fingerprint

Conformations
Catalyst activity
Ethanol
Chymotrypsin
Trypsin
Ions
Calcium
Enzyme Activation
Enzymes
Circular Dichroism
Chemical activation
trypsin drug combination chymotrypsin

Keywords

  • α-Chymotrypsin
  • Calcium ion
  • Ethanol
  • Stability
  • Structure
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Effects of Ca2+ on catalytic activity and conformation of trypsin and α-chymotrypsin in aqueous ethanol. / Kotormán, M.; Laczkó, I.; Szabó, A.; Simon, L. M.

In: Biochemical and Biophysical Research Communications, Vol. 304, No. 1, 25.04.2003, p. 18-21.

Research output: Contribution to journalArticle

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