Investigation on molecular non-covalent interaction in the sodium dodecyl benzene sulfonate-polychrome blue B-protein replacement reaction

Autor:	Rong Shen, Hong-Wen Gao, Ji-Rong Wu
Rok vydání:	2010
Předmět:	Langmuir biology Inorganic chemistry General Chemistry Ovalbumin chemistry.chemical_compound Adsorption Myoglobin chemistry Ionic strength biology.protein Single displacement reaction Bovine serum albumin Ternary operation Nuclear chemistry
Zdroj:	Chinese Journal of Chemistry. 22:798-803
ISSN:	1001-604X
DOI:	10.1002/cjoc.20040220807
Popis:	The molecular non-covalent interaction often originates from the electrostatic attr action and accords with the Langmuir isothermal adsorption. The sodium dodecyl benzene sulfonate (SDBS)-polychrome blue B (PCB)-protein [bovine serum albumin (BSA), ovalbumin (OVA) and myoglobin (MB)] ternary reaction has been investigated at pH 3.88. Protein to replace PCB from the PCB-SDBS binding product was used to characterize the assembly of an invisible-spectral compound, SDBS, on proteins by measuring the variation of PCB light-absorption by the microsurface adsorption-spectral correction (M SASC) technique. The effect of ionic strength and temperature on the aggregation was studied. Results showed that the aggregates SDBS 92BSA, SDBS58OVA and SDBS15MB at 30 and SDBS83BSA, SDBS39OVA and SDBS10MB at 50 are formed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c1a8d6cd25194e0abe8d6be7c095f0b1 https://doi.org/10.1002/cjoc.20040220807 Zobrazit plný text záznamu Plný text