Abstract

Catalase is an antioxidant enzyme with great therapeutic potential that scavenges hydrogen peroxide, a reactive oxygen species produced during cellular metabolism. Substances containing 1,2,4-triazole structures are biologically important heterocyclic compounds found in the structure of many pharmaceutical drugs used in drug discovery studies against various types of diseases in the human body. In this study, the effect of phosphate buffer prepared at different pHs and 3-amino-1,2,4-triazole-5-carboxylic acid (ATZc) on catalase enzyme activity in human blood erythrocytes was determined. It was determined that the catalase enzyme was inhibited by ATZc at different pH levels. The weakest inhibition was observed at pH 5.5 (IC50:49.01 µM), whereas the strongest inhibition was observed at pH 7.5 (IC50:23.21 µM).

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