FEBS Letters · 2004 · 138 citations · 26 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProteomicsEnzyme CharacterizationProteomics IntegrationSecretory PathwayExcretory-secretory AntigensFasciola Hepatica InfectionGel ElectrophoresisProteomic IdentificationSecretory-excretory SystemTwo-dimensional ElectrophoresisTwo-dimensional Gel Electrophoresis
We have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host-parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.
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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Andrej Shevchenko, Matthias Wilm, Ole Vorm et al. · Analytical Chemistry · 1996 · 9.1K citations