TY - JOUR
T1 - Comparative studies of asparagine-linked sugar chains of immunoglobulin G from eleven mammalian species
AU - Hamako, Jiharu
AU - Matsui, Taei
AU - Ozeki, Yasuhiro
AU - Mizuochi, Tsuguo
AU - Titani, Koiti
PY - 1993/12
Y1 - 1993/12
N2 - 1. 1. Asparagine-linked sugar chains released by hydrazinolysis from IgGs of porcine, equine, bovine, goat, ovine, canine, rabbit, guinea-pig and rat were comparatively analyzed by microsequencing and lectin affinity chromatography. 2. 2. Sugar chains of all IgGs basically consisted of biantennary complex-type oligosaccharides containing 0-2 sialic acid residue(s). More than 70% of the oligosaccharides were neutral, except for guinea-pig IgG, and fucosylated trimannosyl core structures were dominant except for rabbit IgG. Bisecting N-acetylglucosamine residue was absent in porcine and equine IgGs. 3. 3. A large quantity of galactose-less oligosaccharides were present in IgGs of porcine, equine, canine and rat.
AB - 1. 1. Asparagine-linked sugar chains released by hydrazinolysis from IgGs of porcine, equine, bovine, goat, ovine, canine, rabbit, guinea-pig and rat were comparatively analyzed by microsequencing and lectin affinity chromatography. 2. 2. Sugar chains of all IgGs basically consisted of biantennary complex-type oligosaccharides containing 0-2 sialic acid residue(s). More than 70% of the oligosaccharides were neutral, except for guinea-pig IgG, and fucosylated trimannosyl core structures were dominant except for rabbit IgG. Bisecting N-acetylglucosamine residue was absent in porcine and equine IgGs. 3. 3. A large quantity of galactose-less oligosaccharides were present in IgGs of porcine, equine, canine and rat.
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U2 - 10.1016/0305-0491(93)90056-B
DO - 10.1016/0305-0491(93)90056-B
M3 - Article
C2 - 8299354
AN - SCOPUS:0027366705
SN - 1096-4959
VL - 106
SP - 949
EP - 954
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 4
ER -