An investigation of protein conformation of cytochrome c by using cytochrome c insolubilized on to agarose gel.
Cytochrome c insolubilized on to agarose gel was shown to be more resistant to denaturation and carboxymethylation than the soluble protein. These differences are discussed both with respect to the conformational changes that take place during denaturation of cytochrome c and with respect to the pH-dependent forms of carboxymethyl-cytochrome c.
D000818:Animals; D003574:Cytochrome c Group / Q000031:analogs & derivatives; D006736:Horses; D006863:Hydrogen-Ion Concentration; D009206:Myocardium / Q000201:enzymology; D009994:Osmolar Concentration; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D012685:Sepharose; D013057:Spectrum Analysis; D014508:Urea / Q000494:pharmacology
D003574:Cytochrome c Group; D014508:Urea; D012685:Sepharose