Protein phosphatase activity in cyanobacteria: Consequences for microcystin toxicity analysis

Abstract

A. T. R. Sim and L.-M. Mudge. Protein phosphatase activity in cyanobacteria: consequences for microcystin toxicity analysis. Toxicon 31, 1179–1186, 1993.—Hepatotoxic microcystin levels in cyanobacteria (blue-green algae) were assessed by an assay based on inhibition of protein phosphatases type 1 (PP1) and type 2A (PP2A) in crude chicken forebrain extracts using 32P-labelled glycogen phosphorylase as substrate. While cyanobacteria are reported to be devoid of phosphorylase phosphatase activity, two samples obtained from cyanobacterial scums, containing predominantly Anabaena circinalis, were found to contain high levels of a phosphorylase phosphatase activity which completely masked the presence of microcystin. Furthermore, samples containing predominantly Microcystis aeruginosa but increasing Anabaena circinalis contained sufficient phosphorylase phosphatase activity to cause a fourfold underestimation of microcystin levels. Thus protocols for microcystin toxicity analysis should take into account the possible presence of endogenous phosphatase activity, thereby preventing underestimation of toxin levels.