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	Provedor de dados BJMBR (2) Autor Günther,A.R. (2) Rogana,E. (2) Santoro,M.M. (2) Bittar,E.R. (1) Caldeira,F.R. (1) Santos,A.M.C. (1) Mais... Palavra-chave Differential scanning calorimetry (1) Protein pH titration (1) Protein stability (1) SS-Trypsin (1) SS-trypsin (1) Thermal denaturation (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2003 (1) 1997 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Characterization of ß-trypsin at acid pH by differential scanning calorimetry BJMBR Bittar,E.R.; Caldeira,F.R.; Santos,A.M.C.; Günther,A.R.; Rogana,E.; Santoro,M.M.. Trypsin is a serino-protease with a polypeptide chain of 223 amino acid residues and contains six disulfide bridges. It is a globular protein with a predominance of antiparallel ß-sheet and helix in its secondary structure and has two domains with similar structures. We assessed the stability of ß-trypsin in the acid pH range using microcalorimetric (differential scanning calorimetry) techniques. Protein concentrations varied in the range of 0.05 to 2.30 mg/ml. Buffer solutions of 50.0 mM ß-alanine and 20.0 mM CaCl2 at different pH values (from 2.0 to 4.2) and concentrations of sorbitol (1.0 and 2.0 M), urea (0.5 M) or guanidinium hydrochloride (0.5 and 1.0 M) were used. The data suggest that we are studying the same conformational transition of the... Tipo: Info:eu-repo/semantics/article Palavras-chave: SS-Trypsin; Thermal denaturation; Differential scanning calorimetry. Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003001200003 pH titration of native and unfolded ß-trypsin: evaluation of the D D G0 titration and the carboxyl pK values BJMBR Günther,A.R.; Santoro,M.M.; Rogana,E.. The stabilizing free energy of ß-trypsin was determined by hydrogen ion titration. In the pH range from 3.0 to 7.0, the change in free energy difference for the stabilization of the native protein relative to the unfolded one (<!-- $MVD$:face("Symbol") -->D D G0 titration) was 9.51 ± 0.06 kcal/mol. An isoelectric point of 10.0 was determined, allowing us to calculate the Tanford and Kirkwood electrostatic factor w. This factor presented a nonlinear behavior and indicated more than one type of titratable carboxyl groups in ß-trypsin. In fact, one class of carboxyl group with a pK = 3.91 ± 0.01 and another one with a pK = 4.63 ± 0.03 were also found by hydrogen ion titration of the protein in the folded state Tipo: Info:eu-repo/semantics/article Palavras-chave: SS-trypsin; Protein stability; Protein pH titration. Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001100003 Registros recuperados: 2 Primeira ... 1 ... Última

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