Multiple myeloma (MM) is an immedicable malignancy of the human plasma cells 
producing abnormal antibodies (also referred to as paraproteins) leading to 
kidney problems and hyperviscosity syndrome. In this paper, we report on the 
N-glycosylation analysis of paraproteins from total human serum as well as the 
fragment crystallizable region (Fc ) and fragment antigen binding (Fab ) κ/λ 
light chain fractions of papain digested immunoglobulins from multiple myeloma 
patients. CE-LIF detection was used for the analysis of the N-glycans after 
endoglycosidase (PNGase F) mediated sugar release and fluorophore labeling 
(APTS). While characteristic N-glycosylation pattern differences were found 
between normal control and untreated, treated and remission stage multiple 
myeloma patient samples at the global serum level, less distinctive changes were 
observed at the immunoglobulin level. Principal component analysis adequately 
differentiated the four groups (control and three patient groups) on the basis 
of total serum N-glycosylation analysis. 12 N-glycan features showed 
statistically significant differences (p <0.05) among various stages of the 
disease in comparison to the control at the serum level, while only six features 
were identified with similar significance at the immunoglobulin level, including 
the analysis of the partitioned Fc fragment as well as the Fab κ and Fab λ 
chains.