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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases
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Animals
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Electrophoresis, Polyacrylamide Gel
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Leishmania tropica / enzymology*
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Metalloendopeptidases / drug effects*
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Solubility
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Tunicamycin / pharmacology*
Substances
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Tunicamycin
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Metalloendopeptidases
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glycoprotein gp63, Leishmania
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase