4',6-diamidino 2-phenylindole is a new reversible inhibitor of diamine oxidase and S-adenosyl-l-methionine decarboxylase from mammalian tissues

Cubría, C.; Alvarez-Bujidos, M.L.; Negro, A.; Balaña‐Fouce, Rafael; Ordóñez, David

doi:10.1016/0742-8413(93)90203-w

Cited by 4 publications

(2 citation statements)

References 15 publications

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“…25 Furthermore, DAPI inhibits trypsin-like serine proteinases, swine kidney copper amine oxidase, and S-adenosyl-L-methionine decarboxylase. 21,26 Preparation of LiposomessNegatively charged liposomes were produced by employing a protocol based on a mechanical hydration step by vortexing, followed by brief ultrasonication and extrusion steps. The liposomal suspension was subjected to five extrusion cycle through two stacked 400-nm pore size polycarbonate filters with homogeneous pore size.…”

Section: Resultsmentioning

confidence: 99%

Cross-Enzyme Inhibition by Gabexate Mesylate: Formulation and Reactivity Study

Cortesi¹,

Ascenzi²,

Colasanti³

et al. 1998

Journal of Pharmaceutical Sciences

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Gabexate mesylate (GM; commercialized under the brand name FOY) is a nonantigenic synthetic inhibitor of plasmatic and pancreatic serine proteinases that is used therapeutically in the treatment of pancreatitis and disseminated intravascular coagulation and as a regional anticoagulant for hemodialysis. The inhibitory effect of GM on nitric oxide synthase as well as serine proteinases and swine kidney copper amine oxidase, all acting on cationic substrates, has been investigated. On the basis of the available X-ray crystal structures of the enzymes considered, the possible binding mode(s) of GM has(have) been analyzed. The enzyme cross-inhibition by GM suggests that the use of this drug should be under careful control. With the aim to improve the scarce plasma stability of GM, the positively charged drug has been complexed to the surface of preformed anionic liposomes. The liposome-complexed GM half-life increases about five-fold, indicating the protective effect of liposomes on GM degradation. Moreover, the GM complexation with liposomes does not alter its inhibitory activity on NOS-I and porcine pancreatic trypsin.

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Section: Resultsmentioning

confidence: 99%

Cross-Enzyme Inhibition by Gabexate Mesylate: Formulation and Reactivity Study

Cortesi¹,

Ascenzi²,

Colasanti³

et al. 1998

Journal of Pharmaceutical Sciences

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“…The structure, expression, activity, and function of porcine DAO were analyzed in several studies [5][6][7][8].…”

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confidence: 99%

Highly Sensitive Determination of DAO Activity by Oxidation of a Luminescence Reagent

Mayer

Pittner

Hermann

et al. 2007

Appl Biochem Biotechnol

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A highly sensitive method for measuring the activity of the enzyme diamine oxidase (DAO) independent of the type of substrate is described. The principle of the assay is to determine the amount hydrogen peroxide generated as a reaction product during oxidation of diamines by DAO. PSatto, a highly sensitive luminescence reagent, was used to generate a signal depending on the hydrogen peroxide concentration based on the action of horseradish peroxidase. DAO is specifically captured from a sample by an antibody immobilized to microwell plates, and the substrate is added to the bound enzyme. Various diamines were used as substrates; the peroxide produced is directly proportional to the amount of DAO bound to the specific antibodies. With this very sensitive method, it is possible to detect pmol amounts of generated hydrogen peroxide in plasma matrix corresponding to the biological activity of DAO.

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