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A neutral cysteine protease of Spirometra mansoni plerocercoid invoking an IgE response.

Authors
Kong, Y | Kang, SY | Kim, SH  | Chung, YB | Cho, SY
Citation
Parasitology, 114(Pt3). : 263-271, 1997
Journal Title
Parasitology
ISSN
0031-18201469-8161
Abstract
When crude extracts of Spirometra mansoni plerocercoid (sparganum) were analysed by SDS-polyacrylamide gel electrophoresis (PAGE)/immunoblot using patients' sera, IgE antibodies reacted specifically with 21, 27 and 53 kDa proteins. The 21 and 27 kDa proteins have been previously characterized as cysteine proteases. In this study, the 53 kDa protein was confirmed, by immunoprecipitation, to induce a specific IgE response. The protein was purified by affinity chromatography using an IgG1 (kappa 2) type mAb. The protein was partially sensitive to peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F (endo F) digestion. It exhibited an endoproteinase activity in a thiol-dependent manner preferentially degrading benzoyloxycarboxyl-phenylalanyl-arginyl-4- methoxy-beta-naphthylamide (Z-phe-arg-MNA) of a panel of substrates tested. This endoprotease activity was maximal at pH 6.5 and in 0.1 M sodium phosphate. The proteolytic activity was inhibited by 10(-5) M L-trans-epoxysuccinyl-L- leucylamido-(4-guanidino)butane (E-64) and 1 mM iodoacetamide (IAA), and potentiated by dithiothreitol (DTT, 5 mM).
MeSH

PMID
9075345
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Pediatrics & Adolescent Medicine
Ajou Authors
김, 성환
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