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Fig. 2. DGN-1 is glycosylated but not cleaved into 
/ß subunits.
(A) Antibodies to DGN-1 regions corresponding to -DG and
ß-DG detect a single major band at 85 kDa (arrow) on western blots of
embryo or mixed larval extracts. The anti-DGN-1ß antibody cross-reacts
with a bacterial antigen in the larval extract (asterisk). (B) DGN-1 is
absent from dgn-1(cg121) lysates probed with
anti-DGN-1, demonstrating that cg121 is a molecular null
allele. The extract from 25 adult animals was run in each lane. (C)
Extracts digested with PNGaseF (protein N-glycosidase F) to remove N-linked
glycans (lanes 2,4) were western blotted with anti-DGN-1 antibody. The
compact 85 kDa species in embryos shifts to 75 kDa after digestion, near to
the predicted polypeptide size. In larval extracts, the broad DGN-1 band
decreases in molecular weight after digestion but remains heterogeneous,
indicating the presence of N-glycosylation and some additional
modification(s), possibly O-glycosylation.
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