Thermal properties of chemically modified cytochrome c.
Differential scanning calorimetry was used as a probe to follow structural disturbances in cytochrome c with electrostatic modification. At 51.7% maleylation, the Td decreased 14.1 degrees C; however, relatively stable delta H values reflected minor structural variations. With 77.5 and 96.4% modification, a significant decrease in delta H was more indicative of major conformational change. On this basis, a critical labelling point was considered. Extensive maleylation (96.4%) did not result in complete cytochrome denaturation. In general, assessment of cytochrome thermal parameters by DSC provided a conformational perspective for the influence of specific electrostatic parameters on molecular integrity.
Ismond
M A
MA
Food Science Department, University of Manitoba, Winnipeg, Canada.
Murray
E D
ED
Arntfield
S D
SD
D000818:Animals; D003574:Cytochrome c Group / Q000032:analysis; D004563:Electrochemistry; D004735:Energy Transfer; D006736:Horses; D006358:Hot Temperature; D008239:Lysine / Q000032:analysis; D009206:Myocardium / Q000201:enzymology; D011487:Protein Conformation
D003574:Cytochrome c Group; D008239:Lysine