salicylates has been researched along with coumarin* in 3 studies
3 other study(ies) available for salicylates and coumarin
| Article | Year |
|---|---|
Vitamin K antagonism of coumarin anticoagulation. A dehydrogenase pathway in rat liver is responsible for the antagonistic effect.
In the liver, it appears that there are two different pathways for vitamin K reduction. One pathway is irreversibly inhibited by coumarin anticoagulant drugs. The other pathway has been shown in the present study to be composed of enzymes that are not effected by physiological 'in vivo' concentrations of these drugs. This pathway appears to be responsible for the antidotal effect of vitamin K in overcoming coumarin poisoning. In rat liver the pathway has been shown to be composed of DT-diaphorase (EC.1.6.99.2) and a microsomal dehydrogenase(s). The activity of the microsomal dehydrogenase(s) was 3.6-fold higher with NADH than with NADPH present in the test system. It appears that this enzyme is the physiologically important enzyme in the pathway. In contrast with DT-diaphorase, this enzyme(s) is shown to be tightly associated with the mirosomal membrane. The enzyme(s) is not identical with either of the quinone-reducing enzymes cytochrome P-450 reductase or cytochrome-b5 reductase. Our data thus postulate the existence of an as-yet-unidentified microsomal dehydrogenase that appears to have an important function in the pathway. Topics: 4-Hydroxycoumarins; Animals; Anticoagulants; Blood Coagulation; Coumarins; Immunosorbent Techniques; Ligases; Male; Microsomes, Liver; NAD(P)H Dehydrogenase (Quinone); Oxidoreductases; Quinone Reductases; Rats; Rats, Inbred Strains; Salicylates; Salicylic Acid; Vitamin K; Warfarin | 1986 |
Hapten binding assay using guinea pig macrophages.
An assay for testing the binding of haptens to antigen-presenting cells was developed. The test consists of consecutive incubation of macrophages with the tested hapten, followed by incubation with a radioactively labeled standard. If the first hapten occupies a certain number of binding sites, the other one (radioactively labeled standard) reveals reduced binding. The binding assay in the present modification is fully suitable for measuring the binding of water-soluble haptens. It was found that from a panel of tested haptens, DNFB, beta-bromostyrol and phenylacetaldehyde exhibit strong binding. Topics: Acetaldehyde; Aldehydes; Animals; Binding, Competitive; Camphor; Coumarins; Dinitrofluorobenzene; Ethanol; Female; Guinea Pigs; Macrophages; Radioligand Assay; Receptors, Antigen; Salicylates; Styrenes; Surface-Active Agents | 1985 |
[Action of lability factor on the effects of sodium salicylate and tromexan on prothrombin time].
Topics: Blood Coagulation Tests; Coumarins; Ethyl Biscoumacetate; Factor V; Prothrombin Time; Salicylates; Sodium Salicylate | 1954 |