Two toxins, a main component A and a minor component B, were isolated from the freshwater cyanobacterium Microcystis aeruginosa (strain 298) and characterized in their chemical structure by amino-acid analysis, configurational analysis, by FAB-MS and 1H-NMR spectroscopy. The acid hydrolysate yielded for toxin A as constituent amino acids D-Ala, L-Leu, D-Glu, erythro-D-beta-Me-Asp and L-Arg, and for toxin B the amino acids D-Ala, L-Leu, D-Glu, erythro-D-beta-Me-Asp and L-Tyr. 1D and 2D 1H-NMR spectroscopy of the toxins A and B in DMSO-d6 allowed to characterize them as cyclic heptapeptides containing both the unusual beta-amino acid Adda (3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid) and N-methyldehydroalanine (Mdha) as additional constituent residues. Toxin A was found to correspond to the known and structurally well characterized microcystin-LR and toxin B to microsystin-LY. The presence of this variant has already been proposed, but its primary structure could be confirmed in this study.