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Siva DV, Gold E, Sankar B, Mcroria N.
“Effect of psychopharmacological agents on DPN-dependent enzymes”.
Fed. Proc.. 1961;20:394 (Part I).
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Abstract
The effect of LSD, BOL, tyramine, phenylisopropyl hydrazide (JB516), 5-hydroxytryptophan (HTP), tryptamine, norepinephrine, d-, and 1-amphetamine, Marsalid etc., on enzymes requiring DPN as a coenzyme was investigated by following the increase in optical density at 340mu in the presence of the proper substrates. A maximum of 10-2M of the compounds was used. Very few of these compounds affected glutamic dehydrogenase except LSD and BOL which showed an inhibition while JB516 showed a small activation. Using yeast alcohol dehydrogenase, HTP, tyramine and tryptamine showed inhibition, while Marsalid and amphetamines were not inhibitory. A freshly prepared solution of JB516 was not inhibitory, but one allowed to stand at room temperature for about 4 hours was markedly so. The fluorescence characteristics also changed. Using liver alcohol dehydrogenase, with vitamin A alcohol or ethyl alcohol as substrate, even a fresh solution of JB516 was inhibitory, while l=amphetamine was much more inhibitory than d-amphetamine. The inhibitory activity of JB516 was reversed by larger amounts of enzyme, or DPN, or by cysteine, showing that the inhibition is probably mediated through blocking of the sulphydryl groups by JB516. Spectrophotofluorimetric evidence for the formation of enzyme-coenzyme and other complexes will be presented.
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