Abstract
Oxidative deamination of β-phenylethylamine or benzylamine by type B monoamine oxidases (MAO) in preparations of sarcoplasmic reticulum vesicles from rabbit skeletal muscles is accompanied by inhibition both of active Ca2+ transport into the vesicles and of the activity of Ca2+, Mg2+-dependent ATPase, which is preventable by deprenil, a specific inhibitor of type B MAO. Aldehydes formed during enzymatic deamination of substrates of type B MAO may perhaps participate in the regulation of Ca2+, Mg2+-dependent ATPase, activity.
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Tat'yanenko, L.V., Raikhman, L.M. & Gorkin, V.Z. Type B monoamine oxidase and functions of Ca2+, Mg2+-dependent adenosinetriphosphatase in preparations from sarcoplasmic reticulum vesicles. Bull Exp Biol Med 83, 317–319 (1977). https://doi.org/10.1007/BF00799348
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DOI: https://doi.org/10.1007/BF00799348