Natural antibodies are glycosylated proteins. In spite of the abundant work on several aspects of protein glycosylation, there is not consent about the role of glycan groups on protein structure and function. The two more widely accepted views are: 1) the glycan group attached to the nascent peptide in the endoplasmic reticulum guaranties the correct folded structure of the peptide. The effect of different degrees and types of glycosylation on the melting temperature of various proteins has been recently quantified ; and 2) the glycan groups have a stabilizing role because they increase the hydrophilicity of the peptide surface (increasing its solubility and inhibiting aggregation). The effect of glycosydation on polypeptide stability and solubility has yet to be determined. In this work we present evidence about the role that glycosylation plays on the stability of human antibodies expressed in corn (an expressing system whose glycosylation machinery may be turn off to avoid the production of a human antibody with the incorrect glycosylation pattern). The practice of shutting down the glycosylation machinery comes to a price as the non glycosylated antibody may be less stable than the glycosylated variety. We have exposed both glycosylated and non glycosylated antibodies to a variety of stresses (including shear, freeze and thaw and high salt concentrations) in the presence and absence of stabilizers (manitol and sucrose). Aggregation was monitored by dynamic light scattering as well as by HPLC using a multiple angle light scattering detector. Changes in secondary structure were monitored by Fourier Transform Infrared Spectroscopy whereas deamidation of glutamine and asparagine residues was monitored by capillary electrophoresis. Our results show that the non glycosylated antibody is more prone to the formation of aggregates induced by freeze and thaw independently of the addition of additives. Moreover, the intrinsic solubility of the non glycosylated antibody was substantially smaller than of the glycosylated variety. There were only marginal differences between changes in secondary structure and in de-amidation.