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XB-ART-27008
Dev Comp Immunol 1989 Jan 01;132:149-57.
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Tryptic digestion of Xenopus IgM and IgY molecules.

Coosemans V , Hadji-Azimi I , Perrenot N .


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Xenopus IgM and IgY molecules were digested by trypsin. Their respective fragments were separated by gel filtration and immunoadsorption. The purified fragments were characterized by SDS-PAGE and immunoblotting. Tryptic digestion of Xenopus IgM resulted in the release, at a low yield, of hexameric Fcmu, and of monovalent Fabmu fragments. The digestion of Xenopus IgY antibodies led to the recovery of divalent and monovalent Fab nu fragments. The antigen-binding property of these fragments was demonstrated. No Fc nu fragments of appreciable size could be detected.

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Species referenced: Xenopus laevis
Genes referenced: ighx prss1