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Sambucus Nigra Lectin is a 150,000 molecular weight tetrameric glycoprotein consisting of four disulfide-linked chains, two of about 36,000 daltons and two of about 38,000 daltons. Sambucus nigra lectin binds preferentially to sialic acid attached to terminal galactose in (a-2,6), and to a lesser degree, (a-2,3), linkage. Binding is also inhibited to some extent by lactose or galactose. This lectin does not appear to bind sialic acid linked to N-acetylgalacto-samine. SNA has been reported to inhibit cell-free protein synthesis.
Agarose bound* Sambucus Nigra Lectin is prepared from affinity-purified lectin. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x107 are used as the solid-phase matrix to which the lectin is covalently bound. The attachment of the lectin to the solid phase is carefully controlled in order to preserve the activity of the lectin as well as to minimize conformational changes of the bound lectin which might result in nonspecific ionic or hydrophobic interactions. |