Titre : |
Thermostabilization of enzymes |
Type de document : |
texte imprimé |
Auteurs : |
Abderrahmane Baghiani, Auteur ; M.V. Park, Directeur de thèse |
Editeur : |
Edinburg [Scotland] : [s.n.] |
Année de publication : |
1987 |
Importance : |
131 f. |
Présentation : |
ill. |
Format : |
29 cm. |
Note générale : |
Master of science : Biological Sciences : Edinburgh, Heriot-watt university : 1987
Bibliogr. f. 123 - 131 |
Langues : |
Anglais (eng) |
Mots-clés : |
Thermostabilization
Enzymes |
Index. décimale : |
Ms00887 |
Résumé : |
Lactate dehydrogenase from rabbit muscle was reacted with a homologous series of dicarboxylic acids of structure HOOC-(CH2)n-COOH, With 0≤ n ≤ 4 under conditions favouring cross-linking via enzyme amino-groups.
Maximal stabilization was observed in the case of succinate (4C atoms).
The data from SDS-polyacrylamide gel electrophoresis indicate only one band corresponding to the monomeric subunit of the enzyme, suggesting the absence of intersubunit cross-linkages. |
Thermostabilization of enzymes [texte imprimé] / Abderrahmane Baghiani, Auteur ; M.V. Park, Directeur de thèse . - Edinburg [Scotland] : [s.n.], 1987 . - 131 f. : ill. ; 29 cm. Master of science : Biological Sciences : Edinburgh, Heriot-watt university : 1987
Bibliogr. f. 123 - 131 Langues : Anglais ( eng)
Mots-clés : |
Thermostabilization
Enzymes |
Index. décimale : |
Ms00887 |
Résumé : |
Lactate dehydrogenase from rabbit muscle was reacted with a homologous series of dicarboxylic acids of structure HOOC-(CH2)n-COOH, With 0≤ n ≤ 4 under conditions favouring cross-linking via enzyme amino-groups.
Maximal stabilization was observed in the case of succinate (4C atoms).
The data from SDS-polyacrylamide gel electrophoresis indicate only one band corresponding to the monomeric subunit of the enzyme, suggesting the absence of intersubunit cross-linkages. |
|