1.
Dev Comp Immunol
; 13(2): 149-57, 1989.
Artigo
em Inglês
| MEDLINE
| ID: mdl-2776935
RESUMO
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.