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Purification and cell attachment activity of a D‐galactose‐binding lectin from the skin of sea hare, Aplysia Kurodai
Author(s) -
Ozeki Yasuhiro
Publication year - 1998
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 - 10.1002/iub.7510450516
Subject(s) - lectin , aplysia , biochemistry , concanavalin a , galactose , affinity chromatography , molecular mass , galectin , chemistry , cell , biology , microbiology and biotechnology , enzyme , in vitro , evolutionary biology
A D‐galactose‐binding lectin which does not require Ca 2+ or reducing reagents to induce activity was purified from skin of sea hare, Aplysia kurodai , by affinity chromatography. Skin lectin was confirmed to be a disulfide‐bonded heteromultimer with molecular mass of 200 kDa, consisting of 28 kDa and 26 kDa subunits by SDS‐PAGE and two‐dimensional SDS‐PAGE. Human rhabdomyosarcoma cells attached to and spread on plastic plates coated with lectin. Cell adhesion induced by lectin was completely inhibited by the addition of lactose.