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Doctoral Thesis
DOI
10.11606/T.54.1992.tde-16032015-113728
Document
Author
Full name
Johnny Rizzieri Olivieri
Institute/School/College
Knowledge Area
Date of Defense
Published
São Carlos, 1992
Supervisor
Committee
Abrego, José Ramon Beltran
Amaral, Lia Queiroz do
Craievich, Aldo Felix
Mascarenhas, Yvonne Primerano
Torriani, Iris C Linares de
Title in Portuguese
Estudo das variações conformacionais das albuminas humana e bovina em solução por espalhamento de raio-x a baixo ângulo
Keywords in Portuguese
Não disponível
Abstract in Portuguese
Soro Alumina bovina (BSA) e humana (HSA) tem um grande interesse biológico devido às suas propriedades como armazenadoras e transportadoras de outras substâncias. Essas proteínas agem também no controle da pressão osmótica do sangue. Elas têm 585 e 582 resíduos de amino-ácidos e pesam aproximadamente 66500 e 66300 daltons, respectivamente. Usando Espalhamento de Raio-x a baixo ângulo, estudamos BSA e HSA nos pH´s entre 2.5 e 7.0. As medidas de intensidade de espalhamento, normalizadas em relação ao feixe incidente, tempo de exposição e espalhamento devido ao solvente e capilar, e corrigidas devido à concentração e à forma do feixe, mostraram uma forte dependência da forma das albuminas com o pH. O raio de giração encontrado apresentou valores entre 26.7Å e 35.0Å e a análise da função distribuição de distâncias P(r) tem mostrado que essas proteínas sofrem uma variação conformacional com o pH. Diferentes modelos teóricos têm sido propostos e analisados, comparando as funções P(r) calculadas dos modelos com as experimentais. A grande variedade de formas encontradas para ambas as proteínas indicam que BSA e HSA são macromoléculas muito flexíveis
Title in English
Not available
Keywords in English
Not available
Abstract in English
Bovine (BSA) and Human Serum Albumin (HSA) have large biological interest due to their storage and Carrier properties of small substances. These proteins act also on the control of the osmotic pressure of the blood. They have 585 and 582 amino-acids residues and weight 66,500 and 66,300 daltons, respectively. Here, we report a Small Angle X-ray scattering (SAXS) study of BSA and HAS on pH between 2.5 and 7.0. The measured scattering intensities, normalized in relation to incident beam, exposition time and scattering dueto solvent and capilar, and corrected due to concentration and beam shape effects, have shown a strong dependence of the protein shape with pH for both albumins. It was found that the radius of gyration varies between 26.7Å and 35.0Å, and the analyses of the distance distribution function, P(r), indicated that these proteins undergoes conformational changes with pH. Different theoretical shapes have been proposed and analysed comparing the computed P(r). A large variety of shapes were found in both proteins, indicating that BSA and HAS are very flexibility macromolecules
 
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Publishing Date
2015-03-16
 
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