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Production and purification of a recombinant human 14 kDa β‐galactoside‐binding lectin
Author(s) -
Hirabayashi Jun,
Ayaki Hitoshi,
Soma Gen-Ichiro,
Kasai Ken-Ichi
Publication year - 1989
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(89)80711-2
Subject(s) - lectin , recombinant dna , masp1 , cd69 , c type lectin , affinity chromatography , biology , microbiology and biotechnology , antigenicity , biochemistry , concanavalin a , complementary dna , molecular mass , antigen , gene , enzyme , in vitro , serine protease , genetics , protease , cytotoxic t cell , il 2 receptor
The cDNA for a 14 kDa human β‐galactoside‐binding lectin was inserted into a plasmid carrying a taq promoter, and the lectin protein was expressed in E. coli cells. The recombinant lectin was extracted from the cells and purified to apparent homogeneity by a single‐step chromatography on an asialofetuin‐agarose column. Subunit molecular mass (14 kDa), hemagglutinating activity and antigenicity were indistinguishable from those of the human placental lectin. Though the N‐terminal of the placental lectin is blocked with an acetyl group, the recombinant lectin was found to have a free amino group. However, the N‐terminal amino acid sequences were identical. The recombinant lectin was considered to have the same three‐dimensional structure as the placental lectin.