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Partial purification and characterization of a cysteine protease Inhibitor from the plerocercoid of Spirometra erinacei

Title
Partial purification and characterization of a cysteine protease Inhibitor from the plerocercoid of Spirometra erinacei
Authors
Chung Y.-B.Yang H.-J.
Ewha Authors
양현종
SCOPUS Author ID
양현종scopus
Issue Date
2008
Journal Title
Korean Journal of Parasitology
ISSN
0023-4001JCR Link
Citation
vol. 46, no. 3, pp. 183 - 186
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
Helminthic cysteine proteases are well known to play critical roles in tissue invasion, nutrient uptake, and immune evasion of the parasites. In the same manner, the sparganum, the plerocercoid of Spirometra mansoni, is also known to secrete a large amount of cysteine proteases. However, cysteine protease inhibitors regulating the proteolytic activities of the cysteine protease are poorly illustrated. In this regard, we partially purified an endogenous cysteine protease inhibitor from spargana and characterized its biochemical properties. The cysteine protease inhibitor was purified by sequential chromatographies using Resource Q anion exchanger and Superdex 200 HR gel filtration from crude extracts of spargana. The molecular weight of the purified protein was estimated to be about 11 kD on SDS-PAGE. It was able to inhibit papain and 27 kDa cysteine protease of spargana with the ratio of 25.7% and 49.1%, respectively, while did not inhibit chymotrypsin. This finding suggests that the cysteine protease inhibitor of spargana may be involved in regulation of endogenous cysteine proteases of the parasite, rather than interact with cysteine proteases from their hosts.
DOI
10.3347/kjp.2008.46.3.183
Appears in Collections:
의학전문대학원 > 의학과 > Journal papers
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