A characterization of abrin A from the seeds of the Abrus precatorius plant.

Abrin A was purified from the seeds of the Abrus precatorius plant and its physical and biological properties were studied. The biological properties of abrin A were found to be similar to the better studied Abrus protein, abrin C, in that it is toxic to cell-free protein synthesis and binds D-galactose. Abrin A contains carbohydrate moieties including both neutral and amine sugars but no metals, similar to the other two Abrus proteins (abrin C and the Abrus agglutinin). Amino acid compositions of the subunits of abrin A indicated that it consists of two different subunits of comparable size. Furthermore, one of the subunits showed microheterogeneity suggesting that abrin A is a mixture of isolectins. A comparative study of abrin A and abrin C based on compositions and tryptic maps reveals them to be closely related. The evidence suggests that the two abrins may have the same mechanisms of toxic action. Far-ultraviolet circular dichroic studies of abrin A show it to contain 47% beta-pleated sheet and 10% alpha-helix, again similar to the other two Abrus proteins.