Related Experiment Video
Updated: Mar 23, 2026

Metabolic Profiling to Determine Bactericidal or Bacteriostatic Effects of New Natural Products using Isothermal Microcalorimetry
Published on: October 29, 2020
Effect of chlorination on the protein phosphatase inhibition activity for several microcystins
H Mash1, A Wittkorn2
1Office of Research and Development, National Risk Management Research Laboratory, Water Supply and Water Resources Division, Treatment Technology Evaluation Branch, United State Environmental Protection Agency, 26 W. Martin Luther King Drive, Cincinnati, OH 45268, USA.
Abstract:
Microcystins are of particular concern due to their toxicity to both humans and animals and may be the most prominent cyanotoxin observed in freshwater. Although a number of studies have investigated the fate of microcystins and other algal toxins through drinking water treatment facilities, measurement of their potential for toxic activity after chlorination, a popular form of treatment in the United States, has not been investigated. In this study, six microcystin variants are subjected to chlorine oxidation. The degradation of each microcystin variant is measured by liquid chromatography/mass spectrometry simultaneously with protein phosphatase inhibition (PPI) response over reaction time with chlorine. Results show that inhibition is dependent on the incorporated amino acid residues, their placement within the microcystin structure, as well as pH. This pH dependence may have practical implications to such activities such as drinking water treatment when the pH is usually adjusted to around 8. Namely, at this pH, even with chlorine addition for disinfection, PPI activity may not be totally eliminated even when the initial MYCs are eliminated.
Related Concept Videos
Anticholinesterase Agents: Poisoning and Treatment
Irreversible agents form a strong bond with the cholinesterase enzyme, making it inactive. The breakdown of the phosphorylated enzyme is...
Microbial Bioremediation of Pesticides
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Antimicrobial Effectiveness

