Purification and characterization of the N-terminal domain of galectin-4 from rat small intestine.
Using affinity chromatography on lactose-agarose, five beta-galactoside binding lectins of 14 to 20 kDa were detected in the rat small intestinal mucosa. The prominant proteins of 17 and 19 kDa were purified to homogeneity by 2D-electrophoresis. Direct N-terminal sequencing of the 17 kDa protein and intrachain sequencing of the 19 kDa protein produced sequences which are part of the N-terminal domain of the L-36/galectin-4. A rabbit polyclonal antibody was raised against the 19 kDa lectin, which specifically recognized the 17 and 19 kDa lectins and detected a related 36 kDa protein in human undifferentiated HT29 cells.
Tardy
F
F
Department of General and Medical Biochemistry, INSERM-CNRS U189, Lyon-Sud Medical School, Oullins, France.
Deviller
P
P
Louisot
P
P
Martin
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002846:Chromatography, Affinity; D037541:Galectin 4; D006388:Hemagglutinins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D006801:Humans; D007413:Intestinal Mucosa / Q000737:chemistry; D007421:Intestine, Small / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008297:Male; D008969:Molecular Sequence Data; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley
D037541:Galectin 4; D006388:Hemagglutinins; D037102:Lectins