Stability of collagen during denaturation.
The stability of calf skin collagen (CSC) type I during thermal and chemical denaturation in the presence of glycerol was investigated. Thermal denaturation of type I collagen was performed in the presence of glycerol or in combination with urea and sodium chloride. The denaturation curves obtained in the presence of urea or sodium chloride retained their original shape without glycerol. These curves were shifted upward proportionally to the glycerol concentration in the reaction medium. This means that glycerol and the denaturants act independently. The explanation is based on the difference in the mechanism of their action on the collagen molecule.
Penkova
R
R
Department of Chemistry and Biochemistry, Medical University, Pleven, Bulgaria.
Goshev
I
I
Gorinstein
S
S
Nedkov
P
P
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D005990:Glycerol / Q000494:pharmacology; D006358:Hot Temperature; D006860:Hydrogen Bonding; D011489:Protein Denaturation; D012867:Skin / Q000737:chemistry*; D012965:Sodium Chloride / Q000494:pharmacology; D014508:Urea / Q000494:pharmacology
D012965:Sodium Chloride; D014508:Urea; D003094:Collagen; D005990:Glycerol