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Jack beans lectin, isolation from

The plant lectin concanavalin A, a metalloprotein isolated from the jack bean, has also received considerable attention. (588-590,630,631) Using the stopped flow NMR technique three distinct conformation states of the protein, when it is bound to Mn, Ca, and a-methyl-D-mannoside, (630) have been deduced. [Pg.89]

Eectins are made up of a group of sugar-binding proteins widely found in plants and animals. Concanavalin A (Con A) is isolated from jack bean Canavalia ensiformis) and is studied extensively among lectins. Con A (molecular mass 104.000) is known to contain four identical binding... [Pg.117]

Concanavalin A, a protein (isolated from jack-beans) which binds carbohydrates and has the general properties of a lectin , agglutinates and inhibits growth of malignant cells (Sharon and Lis, 1972), but it also agglutinates erythrocytes. Each monomeric unit of concanavalin A has one site that binds calcium ions and another that binds Zn ", Co ", or Mn-" ", and both sites must be occupied by the appropriate metal for biological activity to occur. [Pg.485]


See other pages where Jack beans lectin, isolation from is mentioned: [Pg.27]    [Pg.178]    [Pg.186]    [Pg.419]    [Pg.444]    [Pg.186]    [Pg.274]    [Pg.431]    [Pg.137]    [Pg.139]    [Pg.150]    [Pg.186]    [Pg.299]    [Pg.389]   
See also in sourсe #XX -- [ Pg.137 ]




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