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Lectins quaternary structures

Phytohaemagglutinins.—pH-Acetyl]concanavalin A has been shown to bind to, and partially inhibit the enzymic activity of, proline 2-oxoglutaratedioxygenase. The products obtained when concanavalin A is labelled with 4-azidophenyl a-D-mannopyranoside under u.v.-irradiation have been separated by affinity chromatography on Sephadex G-lOO at pH 5. One of the products is a monovalent dimer at pH 5 and a divalent tetramer at pH 7, indicating that photo-affinity labelling did not alter the quaternary structure of concanavalin A, although the haemagglutinating activity of the derivatized lectin was reduced. [Pg.485]

Although the monomeric units of different legume lectins are extremely similar with one another, marked variations have been found in their quaternary structures. [Pg.1648]

In addition to the above quaternary structures, two additional types of legume lectin dimers have been found in the GS-IV and ECorL lectins, which are both dimeric proteins [26]. The peanut lectin, which is a tetramer, has a unique structure composed of two GS-IV type dimers [27]. Such variation in quaternary structure of the legume lectins may be of significance to the role(s) of these lectins in the plant. [Pg.1650]


See other pages where Lectins quaternary structures is mentioned: [Pg.248]    [Pg.248]    [Pg.163]    [Pg.7]    [Pg.2491]    [Pg.2500]    [Pg.236]    [Pg.332]    [Pg.1647]    [Pg.1650]    [Pg.2476]   
See also in sourсe #XX -- [ Pg.11 , Pg.11 , Pg.541 , Pg.543 ]




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Lectins structure

Quaternary structure

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