-LW, and -YR) and nodularin to be distinguished from okadaic acid, calyculin A, and tautomycin. A range of microcystin-and nodularin-containing laboratory strains and environmental samples of cyanobacteria were assayed by CIPPIA, and the results showed good correlation (R 2 ؍ 0.94, P < 0.00001) with the results of high-performance liquid chromatography with diode array detection for toxin analysis. The CIPPIA procedure combines ease of use and detection of low concentrations with toxicity assessment and specificity for analysis of microcystins and nodularins.Cyanobacteria (blue-green algae) produce a wide range of secondary metabolites which are hazardous to humans, livestock, and wildlife (2). Among these are a group of potent hepatotoxins, the microcystins and nodularins. Several bloomforming cyanobacterial genera are capable of producing these toxins; these genera include Microcystis, Anabaena, Planktothrix, and Nostoc, which can produce the cyclic heptapeptide microcystins, and Nodularia, which can produce the cyclic pentapeptide nodularins. The toxins have a number of common structural features, in particular, the unique -C20 amino acid 3-amino-9-methoxy-2, 6,8-trimethyl-10-phenyldeca-4,6-dienoic acid (3, 9).At the molecular level, microcystins bind irreversibly to and inhibit several serine/threonine protein phosphatases, including protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) (17). Reports of animal intoxication and human illness from around the globe (9) and, more recently, the deaths of more than 50 hemodialysis patients in Caruaru, Brazil, have been linked to the presence of microcystins in water (7,11,20). There is a need for increased awareness and enhanced ability to detect these toxins for protection of health and management of bodies of water which are prone to cyanobacterial bloom development (3). Several detection methods are currently in use; these methods include high-performance liquid chromatography (HPLC) (13), small-animal bioassays (5), and enzyme inhibition assays (1, 22). The ability of microcystins to inhibit certain protein phosphatases has led to the development of a number of straightforward assays for detection and quantification of these toxins. Protein phosphatase inhibition assays include the use of 32 P in the form of [ 32 P]glycogen phosphorylase (10, 12) and colorimetric protein phosphatase inhibition assays (1,22). The colorimetric assays may utilize the ability of the catalytic subunit of PP1, as expressed in Escherichia coli (23), to dephosphorylate the chromogenic substrate p-nitrophenylphosphate. However, the protein phosphatase inhibition assays used for detection and analysis of cyanobacterial hepatotoxins also respond to a wide variety of noncyanobacterial toxins and metabolites, including okadaic acid, tautomycin, and calyculin A. The lack of specificity of the protein phosphatase inhibition assays for cyanobacterial hepatotoxins requires that additional confirmatory analytical methods be employed for specific analysis of these toxins. However, th...