Aarhus University Seal / Aarhus Universitets segl

Jens Christian Jensenius

A rainbow trout lectin with multimeric structure

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  • Department of Medical Microbiology and Immunology
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."
Original languageEnglish
JournalComparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology
Pages (from-to)385-90
Number of pages6
Publication statusPublished - 1 Apr 1997

    Research areas

  • Animals, Blotting, Western, Calcium, Carbohydrate Metabolism, Chromatography, Affinity, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Fish Proteins, Lectins, Oncorhynchus mykiss, Sequence Homology, Amino Acid, Substrate Specificity

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