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PubMed1962

Inhibition of cytochrome oxidase by aminoacetonitrile.

Aminoacetonitrile (AAN) decomposes with the formation of a substance that is a potent inhibitor of cytochrome oxidase. The inhibitor is probably cyanide. Connective tissue contains cytochrome oxidase that varies in amount with the maturity of the tissue and is also inhibited by the product of AAN decomposition.

Aminoacetonitrile↗
PubMed1962

Inhibition of the tyrosinase oxidation of one substrate by another.

The catalytic oxidation of catechol by crude preparations of mushroom tyrosinase was studied by a method yielding data on initial reaction velocities. Graphical analysis of the results suggests that an excess of catechol inhibits its own oxidation by a competitive process, thus accounting for the observed optimum in the substrate concentration. However, added phenol, though itself a substrate, inhibits the enzymatic oxidation of catechol by a process that is neither competitive nor non-competitive, but a mixture of the two types. Mechanisms of this inhibition of the enzyme by a second substrate are discussed in exploring the problem of substrate-substrate inhibition.

Catechols↗
PubMed1961

Effects on amine oxidase of substances which antagonize 5-hydroxytryptamine more than tryptamine on the rat fundus strip.

Certain substances, 2-bromolysergic acid diethylamide, dimethyltryptamine (3-(2-dimethylaminoethyl)indole), 2-methyldimethyltryptamine (3-(2-dimethylaminoethyl)-2-methylindole), and 5-benzyloxydimethyltryptamine (5-benzyloxy-3-(2-dimethylaminoethyl)indole), antagonize the effects of 5-hydroxytryptamine on the rat fundus strip more than those of tryptamine. These substances have been tested for their ability to inhibit the oxidation of tryptamine and 5-hydroxytryptamine by suspensions of guinea-pig liver and rat fundus. 2-Bromolysergic acid diethylamide has virtually no inhibitory activity and it is doubtful if the others produce any significant inhibition of amine oxidase in the concentrations which antagonize the effects of 5-hydroxytryptamine more than those of tryptamine. It seems that the differential character of the blocking action of these compounds should be ascribed either to interference with the transport of tryptamine (but not 5-hydroxytryptamine) through the cell wall, coupled with the block of a receptor common to both tryptamine and 5-hydroxytryptamine, or to the existence of separate tryptamine and 5-hydroxytryptamine receptors.The amine oxidases of the guinea-pig liver and rat fundus appear to be a mixture of at least two types of enzyme, one of which has a higher affinity for 5-hydroxytryptamine than the other and is more susceptible to inhibition by 2-methyldimethyltryptamine.

Animals↗