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Alkaline phosphatase from Echinococcus multilocularis: purification and characterization.

M E Sarciron1, W Hamoud, G Azzar

  • 1Département de Parasitologie et de Pathologie Exotique, Université Claude-Bernard, Lyon, France.

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
|January 1, 1991
PubMed
Summary
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Alkaline phosphatase from Echinococcus multilocularis metacestodes differs significantly from host liver enzyme in Vmax, thermal stability, and inhibition patterns, offering potential therapeutic targets.

Area of Science:

  • Biochemistry
  • Parasitology
  • Enzymology

Background:

  • Alkaline phosphatase (ALP) is crucial in various biological processes.
  • Echinococcus multilocularis infection poses significant health risks.
  • Understanding parasite ALP can reveal therapeutic targets.

Purpose of the Study:

  • To characterize and compare alkaline phosphatase from Echinococcus multilocularis metacestodes with host liver ALP.
  • To investigate kinetic, physical, and inhibition properties of both enzymes.

Main Methods:

  • Purification of alkaline phosphatase from parasite metacestodes and gerbil livers.
  • Determination of kinetic parameters (Km, Vmax) using p-nitrophenyl phosphate.
  • Analysis of molecular weight (Mr), isoelectric point (pI), thermal stability, and inhibition by isatin.

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Main Results:

  • Metacestode ALP exhibited a significantly higher Vmax (357 nmol/min/mg) compared to hepatic ALP (6.7 nmol/min/mg).
  • Km values were similar (0.05 mM) for all enzymes.
  • Parasite ALP showed distinct Mr, pI, greater thermal stability, and competitive isatin inhibition, unlike the uncompetitive inhibition in hepatic ALP.

Conclusions:

  • Echinococcus multilocularis alkaline phosphatase is biochemically distinct from the host enzyme.
  • These differences, particularly in Vmax and inhibition, present potential targets for anti-parasitic drug development.