[Purification and chemical study of a Collocalia glycoprotein]

January 17th, 2007


ncbi.nlm.nih.gov

[Article in French]
Houdret N,
Lhermitte M,
Degand P,
Roussel P.

A glycoprotein was purified from the aqueous extract of “edible bird’s nest” (Collocalia) using free flow preparative electrophoresis and represented the main fraction of Collocalia glycoproteins. This glycoprotein is homogeneous upon agarose electrophoresis and slightly polydisperse upon ultracentrifugation (S So 20w = 3,0). The carbohydrate moiety contains galactose, mannose, glucosamine, galactosamine and sialic acid, which is completely released by Clostridium perfringens or Diplococcus pneumoniae neuraminidases and has the same chromatographic behaviour as N-acetyl-neuraminic acid. The peptide part of the glycoprotein is rich in serine, threonine and proline. About 40 p. cent of the hydroxyaminoacids are involved in carbohydrate-peptide linkages.

PMID: 1182216 [PubMed - indexed for MEDLINE

Entry Filed under: Articles

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