A rainbow trout lectin with multimeric structure.
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."
Jensen
L E
LE
Department of Medical Microbiology and Immunology, University of Aarhus, Denmark.
Thiel
S
S
Petersen
T E
TE
Jensenius
J C
JC
D000818:Animals; D015153:Blotting, Western; D002118:Calcium / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002846:Chromatography, Affinity / Q000379:methods; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D029941:Fish Proteins; D037102:Lectins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism*; D017686:Oncorhynchus mykiss / Q000097:blood*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D029941:Fish Proteins; D037102:Lectins; C106303:ladderlectin, Oncorhynchus mykiss; D002118:Calcium