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 Ca 2+-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.
Cammarata, M., Vazzana, M., Chinnici, C., Parrinello, N. (2001). A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1528, 196-202 [10.1016/S0304-4165(01)00193-3].
A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax
CAMMARATA, Matteo;VAZZANA, Mirella;PARRINELLO, Nicolo'
2001-01-01
Abstract
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 Ca 2+-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.
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