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Purification and characterization of the N‐terminal domain of galectin‐4 from rat small intestine
Author(s) -
Tardy F.,
Deviller P.,
Louisot P.,
Martin A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00025-5
Subject(s) - polyclonal antibodies , lectin , galectin , agarose , microbiology and biotechnology , biochemistry , affinity chromatography , chemistry , biology , antibody , enzyme , immunology
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.