A novel beta-galactoside-binding lectin in cultured murine lymphocytic leukemia cells.
Using affinity chromatography on lactosyl-Sepharose, a beta-galactoside-binding protein of 38 kDa was detected in mouse L1210 lymphocytic leukemia cells. Immunoblotting analysis revealed that it is distinct from any known larger molecular weight galectin. The partial amino acid sequences of the 38 kDa protein indicated that it is a novel member of the galectin family. This 38 kDa lectin is expressed in lymphocytic cell lines but not macrophage-like cell lines.
Mai
A
A
Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology. angelam2@cc.tuat.ac.jp
Jung
S K
SK
Tachikawa
H
H
Fujimoto
D
D
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002846:Chromatography, Affinity; D005697:Galactosides; D037161:Galectins; D006388:Hemagglutinins / Q000737:chemistry / Q000302:isolation & purification*; D037102:Lectins / Q000737:chemistry*; D007939:Leukemia L1210; D008214:Lymphocytes; D008264:Macrophages; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured
D005697:Galactosides; D037161:Galectins; D006388:Hemagglutinins; D037102:Lectins