PubMed · 3237088
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M Skinner, A S Cohen. 1988. Amyloid P component.. https://doi.org/10.1016/0076-6879(88)63048-5
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It has previously been shown that in multiple myeloma (MM) each IgG paraprotein exhibits a unique oligosaccharide profile. It has been assumed that this results from a clone specific glycosylation machinery. However, the abnormal physiological environment of the bone marrow in this disease may also affect normal plasma cells producing polyclonal IgG. We present data to show that this is so and that, in two cases, the oligosaccharide profile of the polyclonal IgG reflected that of the paraprotein from the same patient rather than that of normal polyclonal IgG.
Biosynthesis of procaryotic glycoproteins has been studied in some detail only in the extreme halophile Halobacterium halobium. To extend these studies for a moderate halophile, dolichol phosphate-linked oligosaccharides were isolated and characterized from Haloferax volcanii. Mannosyl (beta 1-->4)galactosyl phosphodolichol could be characterized as a main component by GC/MS permethylation analysis, mass spectrometry and 1H-NMR-spectroscopy. Furthermore, two additional components, present in lower quantities, were partially characterized and identified as a tetrasaccharyl phosphodolichol containing mannose, galactose, and rhamnose in the ratio of 2:1:1 as well as another dihexosyl phosphodolichol. Both the latter compounds contain an additional charged group. All these oligosaccharides were found to be linked to a dolichol consisting of 11 or 12 isoprene units including a saturated omega-terminal isoprene residue.