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- W1992600758 abstract "A cDNA encoding the complete precursor of a Fasciola hepatica cathepsin L protease was isolated and sequenced. Functionally active enzyme was expressed and secreted by Saccharomyces cerevisiae transformed with a plasmid carrying the complete gene. Experiments with temperature-sensitive yeast mutants showed that the enzyme is trafficked through the yeast secretory pathway. Yeast transformed with a truncated gene, which lacked the pre-peptide-encoding and most of the pro-peptide-encoding sequences, did not express funtionally active enzyme. The yeast-expressed enzyme exhibited physico-chemical properties in common with the native enzyme including, pH optimum for activity, stability at 37°C and ability to cleave gelatin and immunoglobulin. Enzyme kinetic data showed that the native and yeast-expressed cathepsin L1 have similar specificities for substrates with hydrophobic residues in the P2 position. This is the first report of the functional expression of a cathepsin L proteinase in S. cerevisiae that did not require the use of yeast secretory signal sequences." @default.
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- W1992600758 date "1997-04-15" @default.
- W1992600758 modified "2023-09-27" @default.
- W1992600758 title "Functional Expression of Fasciola Hepatica Cathepsin L1 in Saccharomyces Cerevisiae" @default.
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- W1992600758 doi "https://doi.org/10.1111/j.1432-1033.1997.t01-1-00373.x" @default.
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