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Purification of a 63 kDa β‐d‐galactoside binding lectin from cuttlefish, Todarodes pacificus
Author(s) -
Ozeki Yasuhiro
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201671
Subject(s) - lectin , galectin , galactoside , molecular mass , biochemistry , chemistry , agarose , size exclusion chromatography , affinity chromatography , biology , microbiology and biotechnology , enzyme
A β‐d‐galactoside binding lectin (TPL) was newly purified from the body walls of the cuttlefish, Todarodes pacificus with lactosyl‐agarose affinity column chromatography and reversed‐phase HPLC. Many of the biological properties of the lectin were similar to those of the representative animal β‐d‐galactoside binding lectin, “galectin”. However, with a molecular mass of 63 kDa under reducing and non‐reducing conditions on SDS‐PAGE, TPL is larger than any previously reported galectins. The native molecular mass of TPL was estimated to be about 60 kDa by gel filtration, suggesting that it exists as a monomer and that a single polypeptide containing at least two sugar binding sites. The antisera raised against TPL did not crossreact with bull frog egg galectin‐1, suggesting that TPL is immunologically distinct from the lower vertebrate galectin.