Post-translational modifications of immunoglobulin G: a mouse IgG variant that lacks the entire CH1 domain.
In the present study, we characterized the post-translational modifications of a short-chain variant of mouse IgG2a that lacks the entire CH 1 domain. The short-chain IgG2a and its proteolytic fragments were subjected to electrospray 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 Ga1-GalNAc- at Thr220A in the hinge region. while the Oglycosylation does not occur in its 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 short-chain IgG2a variant is briefly discussed.
Masuda
K
K
Suntory Institute for Bioorganic Research, Mishima-gun, Osaka, Japan. katsuyoshi_masuda@suntory.co.jp
Yamaguchi
Y
Y
Kato
K
K
Kim
H H
HH
Takahashi
N
N
Shimada
I
I
Arata
Y
Y
D000478:Alkylation; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D014644:Genetic Variation; D006031:Glycosylation; D007127:Immunoglobulin Constant Regions / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007074:Immunoglobulin G / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013058:Mass Spectrometry; D051379:Mice; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D016339:Spectrometry, Mass, Fast Atom Bombardment
D007127:Immunoglobulin Constant Regions; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains