FEBS Letters | |
Purification and characterization of the N‐terminal domain of galectin‐4 from rat small intestine | |
Martin, A.1  Deviller, P.2  Tardy, F.1  Louisot, P.1  | |
[1] Department of General and Medical Biochemistry, INSERM-CNRS U189, Lyon-Sud Medical School, BP 12, 69921 Oullins Cedex, France;Molecular and Cellular virology-immunology department, Alexis-Carrel Medical School, Rue G. -Paradin, 69008 Lyon, France | |
关键词: β-Galactoside binding lectin; Galectin; Intestinal mucosa; HT29; EDTA; ethylene diamine tetraacetic acid; 2D-electrophoresis; two-dimensional electrophoresis; PMSF; phenylmethylsulfonyl fluoride; PVDF; polyvinylidene difluoride; PBS; phosphate-buffered saline; SDS-PAGE; sodium dodecylsulfate polyacrylamide gel electrophoresis; TBS; Tris-buffered saline; TST; Tris-buffered saline containing 0.1% Tween 20 and 10% fetal calf serum; | |
DOI : 10.1016/0014-5793(95)00025-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Using affinity chromatography on lactose-agarose, five β-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.
【 授权许可】
Unknown
【 预 览 】
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