Reactivity of polyaminocarboxylatoruthenium(III) complexes with serine and their protease inhibition

Autor:	Reema Bhattacharya, Debasish Bhattacharyya, Susan Basak, Debabrata Chatterjee, Ayon Sengupta, Anannya Mitra
Rok vydání:	2005
Předmět:	chemistry.chemical_classification Serine protease Chymotrypsin Protease biology medicine.medical_treatment Subtilisin Substrate (chemistry) respiratory system Medicinal chemistry Serine Enzyme chemistry Materials Chemistry biology.protein medicine Organic chemistry Reactivity (chemistry) Physical and Theoretical Chemistry
Zdroj:	Journal of Coordination Chemistry. 58:1703-1711
ISSN:	1029-0389 0095-8972
Popis:	Reaction of [Ru(edta)(H2O)]− (edta4− = ethylenediaminetetraacetate), [Ru(pdta)(H2O)]− (pdta4− = propylenediaminetetraacetate) and [Ru(hedtra)(H2O)] (hedtra3− = N-hydroxyethylethylenediaminetriacetate) with S-serine (Ser) was studied spectrophotometrically and kinetically. Serine protease inhibition studies were performed with the three complexes using the serine protease enzymes chymotrypsin and subtilisin with azoalbumin as substrate. Results are discussed in terms of the reactivity of the Ru-pac (pac = polyaminopolycarboxylates) complexes with serine. The order of protease inhibition efficacy of the Ru-pac complexes is [Ru(pdta)(H2O)]− > [Ru(edta)(H2O)]− ≫ [Ru(hedtra)(H2O)], in good agreement with the observed reactivity of Ru-pac complexes with serine.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4a21cf983ae51d6c41058426cae74e11 https://doi.org/10.1080/00958970500247487 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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