Purification and characterization of the N‐terminal domain of galectin‐4 from rat small intestine

FEBS Letters

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