High-mannose type oligosaccharides

Guttman, A. and Pritchett, T., Capillary gel electrophoresis separation of high-mannose type oligosaccharides derivatized by l-aminopyrene-3,6,8-trisul-fonic acid, Electrophoresis, 16, 1906, 1995. 

A saitoi acid carboxypeptidase is a glycoprotein that contains both N- and 0-1 inked sugar chains [81, 82], Glycosylation of the A. saitoi carboxypeptidase suggests the stability of this enzyme against proteinase and proteolysis. In this chapter, the characterization of a new N-linked high-mannose type oligosaccharide from A. saitoi acid carboxypeptidase is described. 

The fete of intravenously admmislered hyaluronidase has been studied in humans and rate using 12iI- or biotin-labeled hyaluronidase. The serum half-life in humans was approximately 3.2 minutes. Similar half-life values have been measured in rets. Within 10 minutes of administration the hulk of the enzyme accumulated in the liver (>5Q ) with measunible minnritiw in the kidneys and spleen. Hie presence of three high-mannose type oligosaccharide subunits per polypeptide chain probably accounts for the rapid uptake by the liver. Pread-... 

SCHEME 11.16 Synthesis of an IL-8 analogue having high mannose-type oligosaccharide. 

Complex carbohydrates released from glycoproteins were readily profiled by capillary gel electrophoresis with LIF-based detection of 1-aminopyrene-3,6,8-trisulfonic acid (APTS)-labeled sugar molecules (Figure 10) [125]. High-mannose-type oligosaccharides of ribonuclease B were derivatized by APTS and separated by capillary electrophoresis using polyethylene oxide separation medium [126]. 

KoUer, A. et al. Analysis of high-mannose-type oligosaccharides by microliquid chromatography-mass spectrometry and capillary electrophoresis. Electrophoresis, 25, 2003, 2004. 

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