6533b7d4fe1ef96bd12628e0
RESEARCH PRODUCT
Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum.
Gigliola BenenatiEric W. OdomNicolò ParrinelloAiti VizziniGerardo R. VastaMatteo CammarataGiuseppina Salernosubject
Serum hemagglutininsTeleostMolecular Sequence DataBiophysicsBiochemistryAffinity chromatographyWestern blotSparus aurataLectinsmedicineAnimalsDicentrarchus labraxAmino Acid SequenceSea bassMolecular BiologyPeptide sequencePolyacrylamide gel electrophoresisbiologyMolecular massmedicine.diagnostic_testSequence Homology Amino AcidLectinF-type lectin; Sparus aurata; Dicentrarchus labrax; Teleost; Serum hemagglutininsbiology.organism_classificationSea BreamBiochemistrybiology.proteinChromatography GelDicentrarchusElectrophoresis Polyacrylamide GelF-type lectindescription
A novel fucose-binding lectin, designated SauFBP32, was purified by affinity chromatography on fucose-agarose, from the serum of the gilt head bream Sparus aurata. Electrophoretic mobility of the subunit revealed apparent molecular weights of 35 and 30 kDa under reducing and non-reducing conditions, respectively. Size exclusion analysis suggests that the native lectin is a monomer under the selected experimental conditions. Agglutinating activity towards rabbit erythrocytes was not significantly modified by addition of calcium or EDTA; activity was optimal at 37 degrees C, retained partial activity by treatment at 70 degrees C, and was fully inactivated at 90 degrees C. On western blot analysis, SauFBP showed intense cross-reactivity with antibodies specific for a sea bass (Dicentrarchus labrax) fucose-binding lectin. In addition, the similarity of the N-terminal sequence and a partial coding domain to teleost F-type lectins suggests that SauFBP32 is a member of this emerging family of lectins.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2007-01-01 | Biochimica et biophysica acta |