The distribution of calmodulin/calmodulin binding proteins in the rat tapeworm, Hymenolepis diminuta.
Live tapeworms have been fixed to retain antigenicity of their proteins, and subsequently prepared for electron microscopy. Thin sections of tapeworms were prepared from resin blocks. Sections were immunocytochemically labelled using a colloidal gold probe and viewed using transmission electron microscopy. Calmodulin was detected associated with cellular structures to which calmodulin has previously been linked in other higher eukaryotes. Calmodulin would appear to have a similar role of importance in tapeworms, as it does in higher eukaryotes although tapeworms are prevalently a syncitium.
Biochemistry Department, Bath University, Claverton Down, U.K.
J L
JL
Eastlake
C J
CJ
Branford-White
W J
WJ
Whish
D000818:Animals; D002147:Calmodulin / Q000032:analysis* / Q000648:ultrastructure; D006926:Hymenolepis / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D008297:Male; D051381:Rats; D017208:Rats, Wistar
D002147:Calmodulin