K. Masuda et al., Post-translational modifications of immunoglobulin G: a mouse IgG variant that lacks the entire C(H)1 domain, MOL IMMUNOL, 36(15-16), 1999, pp. 993-1003
In the present study, we characterized the post-translational modifications
of a short-chain variant of mouse IgG2a that lacks the entire C(H)1 domain
. The short-chain IgG2a and its proteolytic fragments were subjected to ele
ctrosplay ionization- and fast atom bombardment-mass spectrometric analyses
. It has been demonstrated that approximately 14% of the heavy chain of the
short-chain IgG2a is O-glycosylated with a disaccharide of Gal-GalNAc- at
Thr220A in the hinge region, while the O-glycosylation does not occur in it
s parent IgG2a molecule. Two additional modifications have been detected at
the C-termini of both the heavy and light chains of the short-chain IgG2a.
Biological significance of the post-translational modifications of the sho
rt-chain IgG2a variant is briefly discussed. (C) 2000 Elsevier Science Ltd.
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