Abstract
The selective inhibitor of type A monoamine oxidase (MAO) chlorglyline (unlike deprenil, an inhibitor of type B MAO) prevented the appearance of ability to deaminate histamine or AMP, qualitatively new properties for this object, in fragments of mitochondrial membranes from rat liver when incubated under aerobic conditions. The qualitative transformation of the catalytic properties under the influence of oxidizing agents is evidently undergone by type A but not by type B MAO.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature Cited
V. Z. Gorkin, Zh. Vses. Khim. Obshch. im. Mendeleeva, No. 2, 181 (1876).
J. P. Johnston, Biochem. Pharmacol.,17, 1285 (1968).
J. Knoll and K. Magyar, Adv. Biochem. Psychopharmacol.,5, 393 (1972).
T. A. Moskvitina, et al., J. Neurochem.,26, 209 (1976).
N. H. Neff and H.-Y. T. Yang, Life Sci.,14, 2061 (1974).
I. V. Verevkina (Veryovkina) et al., Biochim. Biophys. Acta,258, 56 (1972).
Rights and permissions
About this article
Cite this article
Shatemirova, K.K., Verevkina, I.V. & Gorkin, V.Z. Transformation of mitochondrial monoamine oxidases of types A and B. Bull Exp Biol Med 83, 792–794 (1977). https://doi.org/10.1007/BF00798875
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00798875