Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Laura, Morpurgo"'
Publikováno v:
European Journal of Biochemistry. 271:146-152
For bovine serum amine oxidase, two different mechanisms of substrate-induced inactivation have been proposed. One consists of a slow oxidation by H2O2 of a conserved residue in the reduced enzyme after the fast turnover phase [Pietrangeli, P., Nocer
Autor:
Olivia Befani, Emanuela Masini, Bruno Mondovi, Paola Pietrangeli, Laura Morpurgo, Rodolfo Federico, Mircea Alexandru Mateescu, Enzo Agostinelli
Publikováno v:
InflammoPharmacology. 11:155-163
Two contrasting topics are examined in this account: the protective actions of amine oxidases (AOs) resulting from the elimination and/or modulation of the levels of polyamines and some biogenic amines, such as histamine, in anaphylactic shock and th
Autor:
Giovanni Floris, Bruno Mondovi, Alessandra Padiglia, Laura Morpurgo, Enzo Agostinelli, Rosaria Medda, Andrea Bellelli, Alessandro Finazzi Agrò
Publikováno v:
European Journal of Inorganic Chemistry. 2001:35-42
Publikováno v:
European Journal of Biochemistry. 267:3264-3269
The presteady-state and steady-state kinetics of bovine serum amine oxidase (BSAO) were analyzed by stopped-flow transient spectroscopy. A simplified model of the catalytic cycle was found to describe the experimental data and the rate constants of t
Publikováno v:
Biochemical Journal. 306:697-702
The thermal denaturation of laccase from the Japanese lacquer tree (Rhus vernicifera) was studied by differential scanning calorimetry. The endotherms of holo-laccase, type 2-Cu-depleted laccase and apo-laccase were deconvoluted into two independent
Publikováno v:
Journal of Molecular Structure: THEOCHEM. 330:395-401
Semiempirical AM1 calculations were used to optimize the geometry of the adducts formed by 2,5-dihydroxy- p quinone (DH p Q) with substituted pyridines or imidazole. Hydrogen bond formation was seen to be responsible for the stability of the adducts.
Publikováno v:
Journal of inorganic biochemistry. 109
Lathyrus cicera copper amine oxidase (LCAO) rapidly formed the typical Cu(I)-TPQ semiquinone UV-visible spectrum, identical to that formed by other substrates, upon O(2) exhaustion by turnover with excess tryptamine. A new band at 630 nm formed more
Publikováno v:
Journal of Inorganic Biochemistry. 51:641-647
The crucial point in the selective removal of the type 2 Cu from laccase and ascorbate oxidase by chelating agents was found to be the nature of the reducing agent employed in the reaction. No copper was lost when the reductant was either absent or t
Autor:
Giorgio Stefancich, Enzo Agostinelli, Bruno Mondovi, Luciana Avigliano, Laura Morpurgo, Romano Silvestri, Marino Artico
Publikováno v:
Biochemistry. 31:2615-2621
Aromatic hydrazides of the general formula NH2NHCO(CH2)nC6H4R were covalently bound by bovine serum amine oxidase (BSAO), giving rise to optical and CD absorptions at 350-400 nm. Benzohydrazides (n = 0) reacted slowly, in the ratio of one per dimeric
Publikováno v:
Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology
Scopus-Elsevier
Scopus-Elsevier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fcc54b98e2375db18fee4bcd18c192a
https://doi.org/10.1201/9781420076813.ch5
https://doi.org/10.1201/9781420076813.ch5