Purification of a 63 kDa beta-D-galactoside binding lectin from cuttlefish, Todarodes pacificus.
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.
Ozeki
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Department of System Element, Faculty of Science, Yokohama City University, Japan.
D000818:Animals; D005697:Galactosides / Q000378:metabolism*; D037161:Galectins; D006386:Hemagglutination Tests; D006388:Hemagglutinins / Q000302:isolation & purification* / Q000378:metabolism; D008974:Mollusca / Q000737:chemistry*
D005697:Galactosides; D037161:Galectins; D006388:Hemagglutinins; C007816:beta-galactoside