Subcomponents C1q of the first component of guinea pig and mouse complement. Comparative study of their asparagine-linked sugar chains.
Guinea pig and mouse C1q, subcomponents of the first component of complement, contained six asparagine-linked sugar chains on the C-terminal non-collagenous globular regions of each molecule. After N-acetylation and successive NaB3H4-reduction of asparagine-linked sugar chains liberated by hydrazinolysis, their structure was analysed by sequential exoglycosidase digestion in combination with sugar composition analyses. The sugar chains of C1q molecules of both animals were very similar and composed of the biantennary complex type sugar chains with the following outer chains in various combination is: (+/- NeuNAc alpha leads to)Gal beta 1 leads to GlcNAc beta 1 leads to and Gal beta 1 leads to Gal beta 1 leads to GlcNAc beta 1 leads to. These outer chain moieties were found to be linked to a common core structure of Man alpha 1 leads t o (Man alpha 1 leads to)Man beta 1 leads to GlcNAc beta 1 leads to (Fuc alpha 1 leads to)GlcNAc.
D000818:Animals; D001216:Asparagine; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D003166:Complement Activating Enzymes; D015922:Complement C1q; D006020:Glycopeptides / Q000032:analysis*; D006168:Guinea Pigs; D051379:Mice; D009844:Oligosaccharides / Q000032:analysis*; D013045:Species Specificity
D006020:Glycopeptides; D009844:Oligosaccharides; D001216:Asparagine; D015922:Complement C1q; D003166:Complement Activating Enzymes