title: Exploration of the sea urchin coelomic fluid via combinatorial peptide ligand libraries.
abstract: The urchin Paracentrotus lividus has been characterized via previous capture and enhancement of low-abundance proteins with combinatorial peptide ligand libraries (CPLL, ProteoMiner). Whereas in the control only 26 unique gene products could be identified, 82 species could be detected after CPLL treatment. Due to the overwhelming presence of two major proteins-the toposome (a highly glycosylated, modified calcium-binding, iron-less transferrin) and the major yolk proteins, belonging to the class of cell adhesion proteins-which constituted about 70% of the proteome of this biological fluid and strongly interfered with the capture of the minority proteome, no additional proteins could be detected. Yet, at present, this constitutes the most thorough investigation of the proteome of this biological fluid.
authors.affiliation: Department of Chemistry, Materials and Chemical Engineering Giulio Natta, Politecnico di Milano, Via Mancinelli 7, Milan, Italy.
authors.forename: Elisa
authors.initials: E
authors.lastname: Fasoli
authors.forename: Alfonsina
authors.initials: A
authors.lastname: D'Amato
authors.forename: Pier Giorgio
authors.initials: PG
authors.lastname: Righetti
authors.forename: Rainer
authors.initials: R
authors.lastname: Barbieri
authors.forename: Daniele
authors.initials: D
authors.lastname: Bellavia
mesh_terms: D000818:Animals; D001826:Body Fluids / Q000737:chemistry*; D002352:Carrier Proteins / Q000032:analysis*; D015815:Cell Adhesion Molecules / Q000302:isolation & purification; D020650:Combinatorial Chemistry Techniques; D008024:Ligands; D047328:Paracentrotus / Q000737:chemistry* / Q000145:classification / Q000235:genetics*; D019151:Peptide Library; D040901:Proteomics; D013045:Species Specificity
chemical_list: D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D008024:Ligands; D019151:Peptide Library