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- W3149649463 abstract "The effect of proline hydroxylation on the thermal stability of collagen was investigated.Skin collagen from BN rats with different weeks were separated and purified.The hydroxyproline(Hyp) content in these collagen were analyzed.The influence of hydroxyproline content on the denaturation process of collagen were investigated using the differential scanning calorimeter(DSC) and the circular dichroism(CD)spectroscopy.The CD spectra indicated that collagen obtained from rat skin had the secondary structure typical for collagen.The helix content decreased when denatured by heat treatment.The denaturation temperature and molar enthalpy change was determined using DSC.The results show that the triple-helix become disordered at41.3℃(Tm).The molar enthalpy change increased with quantity of hydroxylation of proline.CD spectrum manifested that part of the triple-helix changed into random coil structure when the denaturation temperature was higher than 41.3℃.The result indicates that the hydroxylation of proline modification is the key factor affecting on the structure of collagen during denaturation process." @default.
- W3149649463 created "2021-04-13" @default.
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- W3149649463 date "2015-01-01" @default.
- W3149649463 modified "2023-09-27" @default.
- W3149649463 title "The Effect of Hydroxylation on the Thermal Stability of Rat Collagen" @default.
- W3149649463 hasPublicationYear "2015" @default.
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