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• W2032055844 abstract "A synthetic gene coding for a chicken egg white cystatin variant was cloned and expressed using the pIN-III-ompA Escherichia coli expression system. After osmotic shock of the E. coli cells, the cysteine proteinase inhibitor was isolated from periplasm and purified by S-carboxymethylpapain affinity chromatography. The resulting inhibitory material was characterized by SDS/PAGE, reversed-phase HPLC, peptide mapping and amino acid sequencing. The recombinant variant chicken AEF-[S1 → M, M29 → I, M89 → L]cystatin shows strong inhibitory activity and displays Ki values in the complex with papain, actinidin and cathepsin B similar to those found for natural chicken cystatin. The purified variant showed a native-chicken-cystatin-like conformational state, as determined by NMR spectroscopy, if the NMR data of 15N-labelled recombinant inhibitor were compared with those of the natural inhibitor." @default.
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• W2032055844 date "1991-08-01" @default.
• W2032055844 modified "2023-09-24" @default.
• W2032055844 title "Purification and characterization of a chicken egg white cystatin variant expressed in an Escherichia coli pIN-III-ompA system" @default.
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• W2032055844 doi "https://doi.org/10.1111/j.1432-1033.1991.tb21059.x" @default.
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