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- W2222634905 abstract "A natural lectin (nominated PjLec) was isolated from haemolymph of the shrimp Penaeus japonicus by affinity chromatography with fetuin-Sepharose. The result of SDS-PAGE showed that the purified PjLec protein consisted of 37kDa subunits. The native PjLec behaved as a 452kDa protein in gel filtration chromatography. Those data suggest that PjLec is composed of 12 subunits of similar molecular weight. PjLec has a broad spectrum of bacterial-agglutination activities against both Gram-positive and Gram-negative bacteria, including two Vibrio species and two other strains pathogenic for shrimp. In addition, PjLec could agglutinate all the vertebrate erythrocytes tested, and the haemagglutination was calcium-independent. The haemagglutination of PjLec was inhibited by ManNAc, Neu5A and lipopolysaccharide. Bovine submaxillary mucin, which contains mainly Neu5A, was the most potent inhibitor of PjLec (MIC of 0.0006mgml(-1)). The haemagglutination activity of PjLec was stable between pH 6 and pH 8, and was temperature-dependent. Our results suggested that PjLec may be an important humoral defence factor against bacterial infection in P. japonicus." @default.
- W2222634905 created "2016-06-24" @default.
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- W2222634905 date "2007-01-01" @default.
- W2222634905 modified "2023-09-28" @default.
- W2222634905 title "Purification and characterisation of a calcium-independent lectin (PjLec) from the haemolymph of the shrimp Penaeus japonicus" @default.
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- W2222634905 doi "https://doi.org/10.1016/j.fsi.2006.03.015" @default.
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