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Monoamine oxidase in rat reticulocytes: Subcellular localization and identification of isoenzymes

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Summary

After “chemically induced reticulocytosis” in rats by treatment with acetyl-phenylhydrazide, monoamine oxidase (MAO) activities were determined in erythrocyte preparations of these animals. Studies on subcellular fractions obtained by differential centrifugation showed that the enzyme activity of rat reticulocytes is a classical mitochondrial MAO.

The patterns of inhibition produced by clorgyline (A-type MAO), deprenil (B-type MAO) and pargyline or tranylcypromine (both types of MAO) in reticulocytes were determined in vitro using tryptamine as a substrate for both types of MAO and phenylethylamine as a substrate for the B-type. The results indicate that both A-type (∼ 75%) and B-type (∼ 25%) MAO are present in rat reticulocytes; while tryptamine was mainly deaminated by the A-type enzyme, both types of MAO were shown to contribute to the deamination of phenylethylamine. These findings were confirmed in investigations on the thermostabilities of the tryptamine and phenylethylamine deaminating activities of rat reticulocyte MAO.

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Authors and Affiliations

  1. Zentrum der Pharmakologie, Klinikum der Universität Frankfurt, D-6000, Frankfurt 70, Germany

    K. Quiring & S. Hubertus

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  1. K. Quiring
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  2. S. Hubertus
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This work was supported by a grant from the Deutsche Forschungsgemeinschaft

The experimental work presented in this paper includes the work done by S. H. for his doctoral thesis

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Quiring, K., Hubertus, S. Monoamine oxidase in rat reticulocytes: Subcellular localization and identification of isoenzymes. Naunyn-Schmiedeberg's Arch. Pharmacol. 300, 273–279 (1977). https://doi.org/10.1007/BF00500970

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  • DOI: https://doi.org/10.1007/BF00500970

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