Purification and characterization of a beta-glucuronidase present during embryogenesis of the mollusk Pomacea sp

Protein Pept Lett. 2005 Oct;12(7):695-700. doi: 10.2174/0929866054696055.

Abstract

A beta-glucuronidase was purified from Pomacea sp. eggs by ammonium sulfate fractionation, DEAE-BioGel and Heparin-Sepharose chromatographies. This enzyme showed a Mr 180 kDa, with subunits of 90 kDa. The kinetic parameters were: pH 4.0, temperature 60 degrees C, Km 2.7 x 10(-6) and Vmax 15.3 microM/h, activator Mg+2, and inhibitor: lactone of D-saccharic acid. beta-glucuronidase is an exoglucuronidase involved in glycosaminoglycans metabolism with kinetics parameters similar to those found in mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Embryonic Development
  • Enzyme Stability
  • Glucuronidase / chemistry
  • Glucuronidase / isolation & purification*
  • Glucuronidase / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Mollusca / classification
  • Mollusca / embryology*
  • Mollusca / enzymology*
  • Temperature

Substances

  • Glucuronidase