Protein complexes present different degrees of stability. We have previously described a glycoprotein from Bacillus thuringiensis that appeared as a multimer unable to be dissociated by the usual SDS-containing sample buffers of pH 6.8. In order to dissociate the complex, a SDS-containing sample buffer of pH 9 was described. In the present report three additional protein complexes with different degrees of stability and the effect of that dissociating sample buffer are described. The study of SDS critical micellar concentration values as a function of pH explains the improvement of dissociating properties at pH 9.
Documento: | Artículo |
Título: | An improvement in the dissociating properties of sodium dodecyl sulfate-containing sample buffers used in polyacrylamide gel electrophoresis. |
Autor: | García-Patrone, M.; Tandecarz, J.S. |
Filiación: | Instituto de Investigaciones Bioquímicas, Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires y CONICET, Argentina |
Palabras clave: | bacterial protein; buffer; dodecyl sulfate sodium; article; chemistry; methodology; micelle; polyacrylamide gel electrophoresis; Bacterial Proteins; Buffers; Electrophoresis, Polyacrylamide Gel; Micelles; Sodium Dodecyl Sulfate |
Año: | 1998 |
Volumen: | 44 |
Número: | 3 |
Página de inicio: | 557 |
Página de fin: | 561 |
Título revista: | Cellular and molecular biology (Noisy-le-Grand, France) |
Título revista abreviado: | Cell. Mol. Biol. (Noisy-le-grand) |
ISSN: | 01455680 |
CAS: | dodecyl sulfate sodium, 151-21-3; Bacterial Proteins; Buffers; Micelles; Sodium Dodecyl Sulfate, 151-21-3 |
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p557_GarciaPatrone |