Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica).
作者： Abinash Chandra MISTRY , Shinji HONDA , Shigehisa HIROSE
DOI: 10.1042/0264-6021:3600107
关键词:
摘要: Using a Japanese-eel (Anguilla japonica) gill cDNA subtraction library, two novel beta-d-galactose-binding lectins were identified that belong to group VII of the animal C-type lectin family. The eel lectins, termed eCL-1 and eCL-2, are simple composed 163 amino acid residues, including 22-residue signal peptide for secretion single carbohydrate-recognition domain (CRD) approximately 130 residues typical lectins. galactose specificity CRD was suggested by presence QPD motif confirmed competitive binding assay. Ruthenium Red staining, shown bind Ca(2+) ions. SDS/PAGE showed native eCL-2 have an SDS-resistant octameric structure (a tetramer disulphide-linked dimers). Northern Western blot analyses demonstrated high-level expression mRNAs their protein products in gills from freshwater eels, which decreased markedly when eels transferred seawater. Immunohistochemistry localized exocrine mucous cells gill.
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