Effect of pH on thermal stability of collagen in the dispersed and aggregated states.
Thermal stabilities of mature insoluble collagen, salt-precipitated fibrils of acid-soluble collagen and acid-soluble collagen in solution were compared as a function of acid pH. Both insoluble and precipitated collagens showed large parallel destabilization with decrease in pH, whereas the intrinsic stability of individual collagen molecules in dilute solution was comparatively unaffected.
D000818:Animals; D001665:Binding Sites; D001965:Bromides; D002417:Cattle; D003094:Collagen; D004355:Drug Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008433:Mathematics; D008854:Microscopy, Electron; D009994:Osmolar Concentration; D011188:Potassium; D011485:Protein Binding; D011489:Protein Denaturation; D012044:Regression Analysis; D012867:Skin
D001965:Bromides; D046911:Macromolecular Substances; D003094:Collagen; D011188:Potassium