Glycosylation sites of hemocyanins of Helix pomatia and Sepia officinalis.
Glycopeptides were isolated from functional units of two molluscan hemocyanins (Hcs). They were analyzed and localized in the sequences. A comparison with potential N-glycosylation sites of two other molluscan Hcs was made. An immunological cross-reactivity was observed between the beta-Hc and the alpha-macroglobulin of Helix pomotia. ELISA experiments with glycopeptide fractions indicated a competition.
Gielens
Constant
C
Laboratory of Biochemistry, Department of Chemistry, Katholieke Universiteit Leuven, B-3001 Leuven, Belgium. constant.gielens@chem.kuleuven.ac.be
De Geest
Natalie
N
Compernolle
Frans
F
Préaux
Gisèle
G
D000818:Animals; D006031:Glycosylation; D006372:Helix, Snails / Q000737:chemistry*; D006433:Hemocyanins / Q000737:chemistry* / Q000276:immunology; D008974:Mollusca / Q000737:chemistry*; D021122:Protein Subunits
D021122:Protein Subunits; D006433:Hemocyanins