Protein involvement in thermally induced structural transitions of pig erythrocyte ghosts.
Thermal transitions in pig erythrocyte ghosts were studied by differential scanning calorimetry and thermal gel analysis (TGA). Heating of the suspension of pig erythrocyte ghosts induced at least six thermodynamically irreversible transitions. Each of these transitions is believed to be due to a localized structural transition induced by thermal stress. Using TGA and covalent attachment of the anionic transport inhibitor regions in the thermograms corresponding to the heat sorption of some proteins of the pig erythrocyte ghosts were identified.
Zhadan
G G
GG
Departamento de Bioquímica y Biología Molecular, Universidad de Salamanca, Spain.
Cobaleda
C
C
Jones
A L
AL
Leal
F
F
Villar
E
E
Shnyrov
V L
VL
D000818:Animals; D001798:Blood Proteins / Q000502:physiology*; D002152:Calorimetry, Differential Scanning; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D013552:Swine; D013816:Thermodynamics
D001798:Blood Proteins