Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid.
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.
Chung
Y B
YB
Department of Parasitology, College of Medicine, Cheju National University, Jeju, 690-756, Korea.
Kong
Y
Y
Cho
S Y
SY
Yang
H J
HJ
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002352:Carrier Proteins / Q000032:analysis* / Q000302:isolation & purification*; D015801:Helminth Proteins / Q000032:analysis* / Q000302:isolation & purification*; D051379:Mice; D008807:Mice, Inbred BALB C; D012911:Snakes / Q000469:parasitology; D013032:Sparganum / Q000302:isolation & purification; D013146:Spirometra / Q000737:chemistry* / Q000254:growth & development / Q000648:ultrastructure*
D002352:Carrier Proteins; D015801:Helminth Proteins; D002118:Calcium