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• W2065402657 endingPage "621" @default.
• W2065402657 startingPage "611" @default.
• W2065402657 abstract "When immunoglobulin G (IgG) was incubated with Spirometra mansoni plerocercoid (sparganum), it was cleaved into Fab and Fc fragments. Fab/c fragments were also hydrolysed. The digestion was accelerated by dithiothreitol (DTT), indicating that cleavage of IgG heavy chain was due to a cysteine protease secreted into the medium. The responsible enzyme, of M r 27 (± 0·8) kDa, was purified by a series of thiopropyl affinity, Sephacryl S-300 HR and DEAE-anion exchange chromatographies, either from worm extracts or from excretory–secretory products (ESP). The purified, thiol-dependent protease showed an optimal activity at pH 5·7 with 0·1 M sodium acetate but was active over the pH range 4·5–8·0. Its activity was inhibited completely by 10 −5 M L-trans-epoxysuccinylleucylamido(4-guanidino) butane (E-64) and 1 mM iodoacetamide (IAA), but by only 53% using the specific cathepsin L inhibitor, Z-Phe-Phe-CHN 2 (5 × 10 −5 M). Partial NH 2 -terminal amino acid sequence was Leu-Pro-Asp-Ser-Val-Asn-Trp-Arg-Glu-Gly-Ala-Val-Thr-Ala-Val which showed 80% homology to human cathepsin S. Immunoblot analysis showed that sera from infected patients exhibited IgE antibody reaction. It is proposed that cleavage of immunoglobulin by an excreted–secreted, cathepsin S-like, allergenic protease is a mechanism of immune evasion used by the sparganum." @default.
• W2065402657 created "2016-06-24" @default.
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• W2065402657 date "1994-12-01" @default.
• W2065402657 modified "2023-09-30" @default.
• W2065402657 title "Cleavage of immunoglobulin G by excretory–secretory cathepsin S-like protease of<i>Spirometra mansoni</i>plerocercoid" @default.
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• W2065402657 doi "https://doi.org/10.1017/s0031182000076496" @default.
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