Abstract
A beta-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 beta-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.
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