A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax

M. Cammarata, M. Vazzana, C. Chinnici, N. Parrinello

Research output: Contribution to journalArticlepeer-review


A lectin specific for fucose and galactose was isolated by affinity chromatography on Sepharose CL-6B from the serum of Dicentrarchus labrax. The hemagglutinating activity against rabbit erythrocytes was calcium-independent, and reached its maximum at 37°C. Two protein components were found in the hemagglutinating fractions eluted from the Sepharose column. Only the 34 kDa component (DLL2) eluted from the polyacrylamide gels (SDS-PAGE) showed agglutinating activity against rabbit erythrocytes. SDS-PAGE, in non-reducing conditions, revealed a single 66 kDa protein that reacted with antibodies to the 34 kDa component. Therefore, a dimeric structure stabilized by disulfide bonds can be proposed. The Ca2+-independent fucose-binding specificity, a significant amino acid sequence homology of the N-terminal trait, and cross-reaction of eel fucolectin with antibodies to DLL2 suggest that this lectin may be included in the recently identified fucolectin family.

Original languageEnglish
Pages (from-to)196-202
Number of pages7
JournalBBA - General Subjects
Issue number2-3
Publication statusPublished - Oct 3 2001


  • Dicentrarchus labrax
  • Fish
  • Fucolectin
  • Hemagglutinin
  • Serum

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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