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	Provedor de dados BJMBR (2) Autor Cortez,C.M. (1) Louro,S.R.W. (1) Silva,D. (1) Wang,N. (1) Ye,L. (1) Yu,J.X. (1) Zhao,B.Q. (1) Mais... Palavra-chave Fluorescence quenching (2) Albumin (1) Bovine serum albumin (1) Chlorpromazine (1) Circular dichroism (1) Efonidipine (1) Hemin (1) Synchronous fluorescence (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Info:eu-repo/semantics/other (1) Ano 2008 (1) 2004 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin BJMBR Silva,D.; Cortez,C.M.; Louro,S.R.W.. The binding of chlorpromazine (CPZ) and hemin to bovine serum albumin was studied by the fluorescence quenching technique. CPZ is a widely used anti-psychotic drug that interacts with blood components, influences bioavailability, and affects function of several biomolecules. Hemin is an important ferric residue of hemoglobin that binds within the hydrophobic region of albumin with high specificity. Quenching of the intrinsic fluorescence of bovine serum albumin (BSA) was observed by selectively exciting tryptophan residues at 290 nm. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern-Volmer graphs were plotted, and the quenching constant estimated for BSA solution titrated with hemin at 25ºC was 1.44 (± 0.05) x... Tipo: Info:eu-repo/semantics/other Palavras-chave: Chlorpromazine; Hemin; Albumin; Fluorescence quenching. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000700004 Spectroscopic studies on the interaction of efonidipine with bovine serum albumin BJMBR Wang,N.; Ye,L.; Zhao,B.Q.; Yu,J.X.. Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA) is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ΔH0 and ΔS0 were 68.04 kJ/mol and 319.42 J·mol-1·K-1, respectively, indicating that the hydrophobic interactions played a major role. The results... Tipo: Info:eu-repo/semantics/article Palavras-chave: Efonidipine; Bovine serum albumin; Fluorescence quenching; Synchronous fluorescence; Circular dichroism. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000700007 Registros recuperados: 2 Primeira ... 1 ... Última

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