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Purification and characterization of the gonad lectin of Aplysia depilans
Author(s) -
Gilboa-Garber Nechama,
Susswein Abraham J.,
Mizrahi Lea,
Avichezer Dody
Publication year - 1985
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(85)80273-8
Subject(s) - lectin , ammonium sulfate precipitation , gonad , biology , biochemistry , molecular mass , sepharose , affinity chromatography , size exclusion chromatography , microbiology and biotechnology , galactose , concanavalin a , endocrinology , in vitro , enzyme
Extracts of gonads and fertilized eggs of Aplysia depilans contain a D‐galacturonic and D‐galactose‐binding lectin. This lectin reacts strongly with rabbit and human erythrocytes independent of ABO blood groups, weakly with dog, mouse, rat, and chick erythrocytes and not at all or very weakly with sheep erythrocytes. Purification of the gonad lectin was easily achieved, with a high yield, by heating to 70°C, precipitation with ammonium sulfate and affinity chromatography on Sepharose 4B. The purified lectin was found to be a glucoprotein of molecular mass around 55–60 kDa; it stimulates mitogenesis of human peripheral lymphocytes.