Metacercarial proteins interacting with WD40-repeat protein of Clonorchis sinensis

The WD40-repeat proteins serve as a platform coordinating partner proteins and are involved in a range of regulatory cellular functions. A WD40-repeat protein (CsWD1) of Clonorchis sinensis previously cloned is expressed stage-specifically in the tegumental syncytium of C. sinensis metacercariae. In...

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Veröffentlicht in:	Korean journal of parasitology 2007-09, Vol.45 (3), p.229-232
Hauptverfasser:	Cho, P.Y. (Chung-Ang University, Seoul, Republic of Korea), Kim, T.I. (Chung-Ang University, Seoul, Republic of Korea), Li, S.Y. (Chung-Ang University, Seoul, Republic of Korea), Hong, S.J. (Chung-Ang University, Seoul, Republic of Korea), E-mail: hongsj@cau.ac.kr, Choi, M.H. (Seoul National University, Seoul, Republic of Korea), Hong, S.T. (Seoul National University, Seoul, Republic of Korea), Chung, Y.J. (Chungbuk National University, Cheongju, Republic of Korea)
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIN ACTINA ACTINE Animals Antibodies, Helminth - metabolism Brief Communication Clonorchis sinensis Clonorchis sinensis - physiology Electrophoresis, Gel, Two-Dimensional - veterinary Helminth Proteins - chemistry Helminth Proteins - isolation & purification Helminth Proteins - metabolism Hydrogen-Ion Concentration Immunoglobulin G - chemistry Microfilament Proteins - chemistry Microfilament Proteins - isolation & purification Microfilament Proteins - metabolism WD40-repeat protein
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Zusammenfassung:	The WD40-repeat proteins serve as a platform coordinating partner proteins and are involved in a range of regulatory cellular functions. A WD40-repeat protein (CsWD1) of Clonorchis sinensis previously cloned is expressed stage-specifically in the tegumental syncytium of C. sinensis metacercariae. In the present study, interacting proteins with the CsWD1 protein was purified by immunoprecipitation and 2 dimension gel electrophoresis from the C. sinensis metacercaria soluble extract, and tryptic peptides were analyzed by LC/ESI-MS.
ISSN:	0023-4001 1738-0006
DOI:	10.3347/kjp.2007.45.3.229