Fugu (Takifugu rubripes) serum GlcNAc-binding lectin is a kalliklectin but has different properties from those of a reported homologue
A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lect...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 2015-09, Vol.158 (3), p.189-195 |
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Sprache: | eng |
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Zusammenfassung: | A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species. |
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ISSN: | 0021-924X 1756-2651 |
DOI: | 10.1093/jb/mvv033 |