ABSTRACT
The glycoproteins was run on SDS-PAGE, the protein bands visualised by coomassie blue and the gel bands cut from the gel. The glycosylation profile of the heavy chain isolated from urine was the same as that from the serum. The labelled glycans were analysed by NPHPLC using an external standard of hydrolysed and 2AB-labelled glucose oligomers, by Weak anion exchange and by liquid chromatography-electrospray ionisation-mass spectrometry LC-ESI-MS. The under-fucosylation of the N-glycans of protein GL-HCDD may render the protein more susceptible to deposition by increased flexibility of the Gal 6’ antenna and thereby revealing amino acids that normally are hidden by the carbohydrate structure and thus lead to enhanced protein-protein interaction that again may lead to protein deposition.
