大鼠小肠中半乳糖凝集素-4 N端结构域的纯化与鉴定

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

作者信息

Tardy F, Deviller P, Louisot P, Martin A

机构信息

Department of General and Medical Biochemistry, INSERM-CNRS U189, Lyon-Sud Medical School, Oullins, France.

出版信息

FEBS Lett. 1995 Feb 13;359(2-3):169-72. doi: 10.1016/0014-5793(95)00025-5.

DOI:10.1016/0014-5793(95)00025-5

PMID:7867792

Abstract

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.

摘要

利用乳糖-琼脂糖亲和层析法，在大鼠小肠黏膜中检测到了5种分子量为14至20 kDa的β-半乳糖苷结合凝集素。通过二维电泳将17 kDa和19 kDa的主要蛋白质纯化至同质。对17 kDa蛋白质进行直接N端测序，对19 kDa蛋白质进行链内测序，所得序列是L-36/半乳糖凝集素-4 N端结构域的一部分。制备了针对19 kDa凝集素的兔多克隆抗体，该抗体可特异性识别17 kDa和19 kDa凝集素，并在人未分化的HT29细胞中检测到一种相关的36 kDa蛋白质。