The solubilities of denatured proteins in different organic solvents.
Acta Chem Scand (Cph)
; 53(12): 1122-6, 1999 Dec.
Article
em En
| MEDLINE
| ID: mdl-10629937
ABSTRACT
The solubilities of heat-denatured and reduced, S-carboxymethylated proteins have been investigated in various organic solvents. Polar, protic solvents (formic acid, trifluoroacetic acid, 3-mercaptopropionic acid) were found to be good solvents for the denatured proteins (20-40 mg ml-1), and the solubilities of the reduced, S-carboxymethylated proteins were generally higher than those of the heat-denatured forms. Most other organic solvents were less effective in solubilizing the denatured proteins. Apolar solvents did not solubilise denatured proteins, but low solubilizing powers were observed for polar, aprotic solvents. Heat-denaturation was observed to result in the formation of large intermolecular aggregates, which, for ovalbumin and lysozyme, were formed by intermolecular S-S bonds, but for bovine serum albumin involved intermolecular isopeptide bonds.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
Idioma:
En
Revista:
Acta Chem Scand (Cph)
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Dinamarca