Secondary structural changes of homologous proteins, lysozyme and α-lactalbumin, in thermal denaturation up to 130 °C and sodium dodecyl sulfate (SDS) effects on these changes : comparison of thermal stabilities of SDS-induced helical structures in these proteins

The thermal stability of two homologous proteins, lysozyme and α-lactalbumin, was examined by circular dichroism. The present study clearly showed two different aspects between the homologous proteins: (1) the original helices of lysozyme and α-lactalbumin were unchanged at heat treatments up to 60...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 28(2012), 47 vom: 27. Nov., Seite 16268-73
1. Verfasser: Moriyama, Yoshiko (VerfasserIn)
Weitere Verfasser: Kondo, Naoaki, Takeda, Kunio
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Comparative Study Journal Article Sodium Dodecyl Sulfate 368GB5141J Lactalbumin 9013-90-5 Muramidase EC 3.2.1.17