[Effect of corticotropin on the dehydrogenase activity of cells and tissues].
The authors studied the effect of native ACTH on dehydrogenase activity of isolated strips of rat diaphragm and suspension of E. coli cells, serotype O III:B4, grown on beef extract agar in a medium with different dehydrogenation substrates. ACTH activated dehydrogenase of rat diaphragm in a medium containing pyruvate, alpha-ketoglutarate, malate, beta-hydroxybutyrate, D-aspartic acid and did not alter it in a medium containing succinate. In contradistinction to rat diaphragm, ACTH activated dehydrogenase of E. coli cells whatever the substrates used (oxaloacetate, isocitrate, alpha-ketoglutarate, succinate, fumarate, malate, pyruvate, lactate, beta-hydroxybutyrate, glucose, D-aspartic acid. Synacthen (ACTH1-24) exerted a similar effect. It is suggested that the effects of ACTH are mediated via its influence on adenylate cyclase in the absence of receptors.
Korkach
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Gudz'
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D000324:Adrenocorticotropic Hormone / Q000494:pharmacology*; D000818:Animals; D002952:Citric Acid Cycle / Q000187:drug effects; D003964:Diaphragm / Q000187:drug effects / Q000201:enzymology; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology; D066298:In Vitro Techniques; D008297:Male; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats
D000324:Adrenocorticotropic Hormone; D010088:Oxidoreductases
Vliianie kortikotropina na degidrogenaznuiu aktivnost' kletok i tkaneĭ.