The effect of tunicamycin on the protease activity of GP63 from Leishmania major

Mol Biol Rep. 1992 May;16(2):81-4. doi: 10.1007/BF00419752.

Abstract

The protease activity of gp63 from L. major was studied in relation to tunicamycin induced N-deglycosylation. It was found that after tunicamycin treatment, a N-deglycosylated product of gp63 with protease activity is present at the cell surface of Leishmania promastigote.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases
  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Leishmania tropica / enzymology*
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Metalloendopeptidases / drug effects*
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Solubility
  • Tunicamycin / pharmacology*

Substances

  • Tunicamycin
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Metalloendopeptidases
  • glycoprotein gp63, Leishmania
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase