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PubMed · 9149391

A rainbow trout lectin with multimeric structure.

L E Jensen·S Thiel·T E Petersen·J C Jensenius
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Abstract

A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetyl-mannosamine, L-fucose, maltose and alpha-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser degree and mannosamine and galactose do not inhibit the binding to Sepharose. When analysed by SDS-PAGE under non-reducing conditions, the lectin appears as a characteristic ladder of bands with approximately 16 kDa between consecutive bands. Upon reduction, the lectin appears as a 16-kDa band. On size-exclusion chromatography of trout serum and plasma, the protein emerges over a broad range corresponding to sizes from about 2000 kDa to less than 200 kDa. The NH2-terminal sequence (AAENRNQXPPG) shows no significant homology with known proteins. Because of the characteristic appearance in non-reducing SDS-PAGE and the lectin activity, we propose to name the protein "ladderlectin."

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AnimalsBlotting, WesternCalciumCarbohydrate MetabolismChromatography, AffinityChromatography, LiquidElectrophoresis, Polyacrylamide GelFish ProteinsLectinsOncorhynchus mykissSequence Homology, Amino AcidSubstrate SpecificityJournal ArticleResearch Support, Non-U.S. Gov't

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L E Jensen, S Thiel, T E Petersen, J C Jensenius. 1997. A rainbow trout lectin with multimeric structure.. https://doi.org/10.1016/s0305-0491(96)00273-8

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