The sexuality-inducing glycoprotein of Volvox carteri f. nagariensis was purified from supernatants of disintegrated sperm packets of the male strain IPS-22 and separated by reverse-phase HPLC into several isoforms which differ in the degree of O-glycosylation. Total chemical deglycosylation with trifluoromethanesulphonic acid yields the biologically inactive core protein of 22.5 kDa. This core protein possesses three putative binding sites for N-glycans which are clustered in the middle of the polypeptide chain. The N-glycosidically bound oligosaccharides were obtained by glycopeptidase F digestion and were shown by a combination of exoglycosidase digestion, gaschromatographic sugar analysis and two-dimensional HPLC separation to possess the following definite structures: (A) Man β1-4GlcNAc β1-4GlcNAc; (B) (Man α)3 Man β1-4GlcNAc β1-4GlcNAc Xyl β; (C) (Man α)2 Man β1-4GlcNAc β1-4GlcNAc; (D) (Man)2Xyl(GlcNAc)2. Xyl β Two of the three N-glycosidic binding sites carry one B and one D glycan. The A and C glycans are shared by the third N-glycosylation site. The O-glycosidic sugars, which make up 50% of the total carbohydrate, are short (up to three sugar residues) chains composed of Ara, Gal and Xyl and are exclusively bound to Thr residues.

• Compound ID: 16894
  

  b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc

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  Structure type: oligomer
  Compound class: N-glycan
  Reference(s) to other database(s): GTC:G34463WT, CCSD:4838, CBank-STR:5078, EMBL:X05776 VCIND
  
   
  
  Volvox carteri f. nagariensis
  CSDB ID 123457 (all data & tools)