Physical studies on three lectins from the seeds of Abrus precatorius.
The physical properties of three lectins from the seeds of the Abrus precatorius plant, abrin C, abrin A and the Abrus agglutinin, were studied. All three exhibited similar circular dichroic (CD) spectra in the near-ultraviolet having negative maxima at 286 and 293 nm. In addition, D-galactose induced similar conformational alterations in the three proteins as observed through changes in the near-ultraviolet CD from 280 to 295 nm. The near-ultraviolet CD spectrum of the toxic subunit of abrin C was very different from that of the parent molecule. The fluorescence emission spectra of the three proteins were also studied. All exhibited fluorescence near 335 nm which is quenched 9% by galactose. Iodide quenching of fluorescence using the Stern-Volmer analysis indicated different tryptophan accessibilities in the presence and absence of D-galactose for the Abrus agglutinin. The results suggest that there is a saccharide-induced conformational change which buries several partially exposed tryptophan residues. A comparable analysis of the closely related Ricinus agglutinin revealed that its tryptophan residues are more buried than those of the Abrus agglutinin and, unlike the Abrus agglutinin, there was no saccharide-induced change in tryptophan accessibility.
D000036:Abrin / Q000031:analogs & derivatives / Q000032:analysis*; D002942:Circular Dichroism; D007887:Fabaceae / Q000032:analysis; D005690:Galactose / Q000494:pharmacology; D007454:Iodides / Q000494:pharmacology; D037102:Lectins / Q000032:analysis*; D037121:Plant Lectins; D010940:Plant Proteins / Q000032:analysis*; D010944:Plants / Q000032:analysis*; D010946:Plants, Medicinal; D010947:Plants, Toxic; D011487:Protein Conformation / Q000187:drug effects; D012278:Ricinus / Q000032:analysis; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis
D007454:Iodides; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D000036:Abrin; D014364:Tryptophan; D005690:Galactose