title: Fasciola hepatica: rapid identification of newly excysted juvenile proteins.
abstract: The sensitivity of N-terminal sequencing has been used to identify proteins expressed by the newly excysted juvenile stage of the parasite Fasciola hepatica. Of the seven proteins identified, a number have significant sequence homology to the cysteine proteases: cathepsin B, cathepsin L and asparaginyl endoproteinase. Proteolytic activity was demonstrated using gelatin substrate sodium dodecyl sulphate polyacrylamide gel electrophoresis. In addition, a number of novel proteins were identified which shared no significant sequence homology to proteins in the databases. The availability of such N-terminal sequence information allows rapid identification of major proteins from scarce developmental stages and provides the basis for further molecular studies.
authors.affiliation: Centre for Animal Biotechnology, University of Melbourne, School of Veterinary Science, Parkville, Victoria, Australia.
authors.forename: J
authors.initials: J
authors.lastname: Tkalcevic
authors.forename: K
authors.initials: K
authors.lastname: Ashman
authors.forename: E
authors.initials: E
authors.lastname: Meeusen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003546:Cysteine Endopeptidases / Q000096:biosynthesis / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005210:Fasciola hepatica / Q000378:metabolism*; D005780:Gelatin; D015801:Helminth Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012680:Sensitivity and Specificity; D017386:Sequence Homology, Amino Acid
chemical_list: D015801:Helminth Proteins; D005780:Gelatin; D003546:Cysteine Endopeptidases