Abstract
Seven cathepsin B-like cysteine proteases (CBLs) were identified from the immunoprotective excretory-secretory products of Haemonchus contortus. Two-dimensional (2-D) zymography and biotinylated inhibitors were employed to localize active CBLs in 2-D protein gels. Mass spectrometry provided the identification of AC-4, HMCP1, HMCP2, and GCP7 as well as three novel CBLs encoded by clustered expressed sequence tags.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Biotinylation / methods*
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Cysteine Endopeptidases / isolation & purification*
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Cysteine Endopeptidases / metabolism
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Electrophoresis, Polyacrylamide Gel
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Haemonchiasis
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Haemonchus / enzymology*
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Helminth Proteins / isolation & purification
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Helminth Proteins / metabolism*
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Mass Spectrometry
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Molecular Sequence Data
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Sequence Alignment
Substances
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Helminth Proteins
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Cysteine Endopeptidases