A method for investigating the effect of temperature on the 695 nm band of insoluble cytochrome c.
A method is described for computer analysis of simple spectrophotometric changes in particulate systems, and this has been applied to the bleaching of the 695 nm band of insoluble ferricytochrome c by temperature. The results show that insolubilization has no effect on the standard enthalpy change but lowers the value for the standard entropy change. This effect appears to be independent of the concentration of the gel matrix to which the cytochrome c is bound, but dependent on the ionic strength of the surrounding solution.
D000818:Animals; D002151:Calorimetry; D003201:Computers; D003574:Cytochrome c Group; D006736:Horses; D008433:Mathematics; D009206:Myocardium / Q000201:enzymology; D011485:Protein Binding; D011487:Protein Conformation; D012685:Sepharose; D012965:Sodium Chloride; D012995:Solubility; D013053:Spectrophotometry; D013696:Temperature; D013816:Thermodynamics
D003574:Cytochrome c Group; D012965:Sodium Chloride; D012685:Sepharose