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The identification and characterization of xenoantigenic nonhuman carbohydrate sequences in membrane proteins from porcine kidney
Author(s) -
Kim YunGon,
Kim SunYoung,
Hur YoungMi,
Joo HwangSoo,
Chung Junho,
Lee DongSup,
Royle Louise,
Rudd Pauline M.,
Dwek Raymond A.,
Harvey David J.,
Kim ByungGee
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500275
Subject(s) - glycan , fucose , biochemistry , mannose , chemistry , glycoprotein , galactose , membrane protein , carbohydrate conformation , biology , membrane , polysaccharide
The immunogenic nonhuman carbohydrate sequences in membrane proteins from porcine kidney were identified and characterized using MALDI‐TOF MS and ESI‐QTOF‐MS. The MALDI profile, investigated by incubation with exoglycosidases, showed a series of about 40 carbohydrates that were identified as high mannose glycans (Man 3–9 GlcNAc 2 ) and complex bi‐, tri‐, and tetra‐antennary glycans with and without core fucose. The antennae of many of the complex glycans were terminated with α‐galactose residues, with the numbers of these residues ranging from one up to the number of antennae. Negative ion ESI‐MS/MS spectra confirmed the location of the α‐galactose residues on the ends of the antennae. This total glycan profile of the membrane proteins from porcine kidney will thus provide important information for the study of molecular interactions between antigenic carbohydrates and proteins in xenotransplantation.