Abstract
A lectin from the alga Codium giraffa, reported as an endemic species of Mexico, was purified by a combination of ammonium sulfate fractionation, affinity and anion exchange chromatographies. Giraffine, as we called this lectin, shares some characteristics with other lectins isolated from the same genus. It is a monomeric protein with a relative molecular weight of 17,800, as shown by native and SDS-PAGE and confirmed by mass spectrometry; its isoelectric point was 6.4 and it did not show multiple molecular forms. The agglutinating activity of this lectin was inhibited with low concentrations of N-acetylglucosamine and N-acetylgalactosamine and was independent of divalent cations.
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