Salting-out is related to the hydrophobic patches close to the protein surface and the removal of the hydration layers around proteins. For glycoproteins that are "hard to precipitate", could the glycosylated part of the molecule contribute with that behavior, i.e. could interfere with the precipitation? For me it seems plausible.
I agree with you, the glycosylation pattern can change the solubility of a protein. Here are some references that may help. Regards.
Adapting protein solubility by glycosylation.: N-Glycosylation mutants of Coprinus cinereus peroxidase in salt and organic solutions
http://www.sciencedirect.com/science/article/pii/S016748389900103X
Covalent binding of glycosyl residues to .beta.-lactoglobulin: effects on solubility and heat stability
http://pubs.acs.org/doi/abs/10.1021/jf00061a036
Effects of glycosylation on the stability of protein pharmaceuticals
http://onlinelibrary.wiley.com/doi/10.1002/jps.21504/full
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