Some physicochemical and enzymic properties of selenium-containing abzyme

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1645-50. doi: 10.1006/bbrc.1994.2122.

Abstract

We successfully prepared the Se-containing abzyme (Se-abzyme) with glutathione peroxidase (GPX) activity and further studied its physicochemical and enzymic properties and stabilities. Data showed that the isoelectric point of the abzyme was 6.95-7.08, and its molecular weight was 158 KD. The ranges of optimum pH and temperature of the Se-abzyme were wider than the native GPX. The store stability of the abzyme was higher than the native GPX. The Se content in the abzyme was found to be 5 mol Se/mol abzyme by X-ray photoelectron spectrum, and binding constant 1.11 x 10(7)M-1 by using ELISA method. The Se-abzyme was inhibited competitively by dithiobis(2-nitrobenzoic acid) (DTNB), and inhibition constant was determined to be 1.25 x 10(-3)M-1.

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Stability
  • Enzymes / chemistry*
  • Enzymes / metabolism*
  • Glutathione / metabolism
  • Glutathione Peroxidase / antagonists & inhibitors
  • Glutathione Peroxidase / chemistry*
  • Glutathione Peroxidase / metabolism
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Molecular Weight
  • Mutation
  • Selenium / analysis*
  • Substrate Specificity
  • Temperature

Substances

  • Enzymes
  • Glutathione Peroxidase
  • Glutathione
  • Selenium