Abstract
The unit A-type glycopeptides were purified from porcine thyroglobulin by Pronase digestion followed by chromatography on a DEAE-Sephadex A-25 column. These glycopeptides were separated into five fractions (UA-I, -II, -IV and -V) by Dowex 50W (X2) column chromatography. Fractions UA-I, -II, -III, -IV and -V were found to have the compositions (Man)9(GlcNAc)2-Asn, (Man)8(GlcNAc)2-Asn, (Man)7(GlcNAc)2-Asn, (Man)6(GlcNAc)2-Asn and (Man)5(GlcNAc)2-Asn respectively. The structures of these five fractions were investigated by the combination of exo- and endo-glycosidase digestions, methylation analysis. Smith periodate degradation and acetolysis. The results showed that fraction UA-V had the simplest structure: see formula in text. The larger glycopeptides (fractions UA-I, -II, -III and -IV) contained additional mannose residues alpha (1 leads to 2)-linked to the terminal mannose residues in the above core structure. These unit A-type glycopeptides appear to be biosynthetic intermediates that are to be processed to form complex-type glycopeptides (unit B-type sugar chains).
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