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Title: Quinoline and quninaldine as naturally occurring inhibitors specific for type A monoamine oxidase. Author: Naoi M, Nagatsu T. Journal: Life Sci; 1987 Mar 16; 40(11):1075-82. PubMed ID: 3821373. Abstract: Type A monoamine oxidase (MAO-A) in human placental mitochondria was competitively inhibited by naturally occurring substances, quinoline and quinaldine, using kynuramine as substrate. Quinoline had a higher affinity for MAO than kynuramine. MAO-A in human brain synaptosomal mitochondria was also competitively inhibited by quinoline, while type B MAO (MAO-B) was reversibly and non-competitively inhibited by quinoline. Quinoline inhibited MAO-A much more potently than MAO-B. Of several compounds structurally similar to quinoline, isoquinoline noncompetitively inhibited MAO-A and -B activity.[Abstract] [Full Text] [Related] [New Search]