Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid

Y. B. Chung; Y. Kong; S. Y. Cho; H. J. Yang

doi:10.1007/s00436-002-0694-4

Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid

Y. B. Chung, Y. Kong, S. Y. Cho, H. J. Yang

Department of Parasitology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

In cestode parasites, calcareous corpuscles are thought to be associated with a number of intracellular physiologies by regulating the trafficking of mineral components. We previously separated these particular components by Ficoll, and their binding proteins of 10 kDa and 35 kDa in the Spirometra mansoni plerocercoid (sparganum). In the present study, we purified a 10 kDa protein employing octyl-Sepharose CL-4B affinity chromatography. Anti-serum raised against the purified protein showed specific reactions to the calcareous corpuscles of the worm section by immunohistochemistry, and recognized the 10 kDa protein by immunoblotting.

Original language	English
Pages (from-to)	235-237
Number of pages	3
Journal	Parasitology Research
Volume	89
Issue number	3
DOIs	https://doi.org/10.1007/s00436-002-0694-4
State	Published - 1 Feb 2003

Bibliographical note

Funding Information:
Acknowledgement This work was supported by a Korea Research Foundation Grant (KRF-2000-00-F00054).

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title = "Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid",

abstract = "In cestode parasites, calcareous corpuscles are thought to be associated with a number of intracellular physiologies by regulating the trafficking of mineral components. We previously separated these particular components by Ficoll, and their binding proteins of 10 kDa and 35 kDa in the Spirometra mansoni plerocercoid (sparganum). In the present study, we purified a 10 kDa protein employing octyl-Sepharose CL-4B affinity chromatography. Anti-serum raised against the purified protein showed specific reactions to the calcareous corpuscles of the worm section by immunohistochemistry, and recognized the 10 kDa protein by immunoblotting.",

author = "Chung, {Y. B.} and Y. Kong and Cho, {S. Y.} and Yang, {H. J.}",

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AU - Kong, Y.

AU - Cho, S. Y.

AU - Yang, H. J.

N1 - Funding Information: Acknowledgement This work was supported by a Korea Research Foundation Grant (KRF-2000-00-F00054).

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N2 - In cestode parasites, calcareous corpuscles are thought to be associated with a number of intracellular physiologies by regulating the trafficking of mineral components. We previously separated these particular components by Ficoll, and their binding proteins of 10 kDa and 35 kDa in the Spirometra mansoni plerocercoid (sparganum). In the present study, we purified a 10 kDa protein employing octyl-Sepharose CL-4B affinity chromatography. Anti-serum raised against the purified protein showed specific reactions to the calcareous corpuscles of the worm section by immunohistochemistry, and recognized the 10 kDa protein by immunoblotting.

AB - In cestode parasites, calcareous corpuscles are thought to be associated with a number of intracellular physiologies by regulating the trafficking of mineral components. We previously separated these particular components by Ficoll, and their binding proteins of 10 kDa and 35 kDa in the Spirometra mansoni plerocercoid (sparganum). In the present study, we purified a 10 kDa protein employing octyl-Sepharose CL-4B affinity chromatography. Anti-serum raised against the purified protein showed specific reactions to the calcareous corpuscles of the worm section by immunohistochemistry, and recognized the 10 kDa protein by immunoblotting.

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Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid

Abstract

Bibliographical note

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