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- W2361443215 abstract "Objective To study the thermostability,circular dichroism and infrared spectral characteristics of type Ⅱ collagen purified from cartilage of Prionace glauca.Methods The digestion of pepsin was applied to extract type Ⅱ collagen from Prionace glauca cartilage.SDS-PAGE、DSC、CD andIR were used to analyze type Ⅱ collagen relative molecular mass、thermal denaturation temperature、secondary structure and infrared spectral characteristics respectively.Results The type Ⅱ collagen from Prionace glauca was composed of α1 chains with relative molecular mass 130kDa.The thermal denaturation temperature of Prionace glauca type Ⅱ collagen was 40.5 ℃,and and could alter its thermostability.IR analysis indicated that the characteristic absorption peaks of Prionace glauca type Ⅱ collagen were at 3411、3008、1648 and 1549cm-1.β-sheet was the main secondary structure of Prionace glauca type Ⅱ collagen,and its ratio was 36.9%,which was close to all-β-type tertiary structure. could change its secondary structure element ratio.With the additive amount of ,β-sheet disappeared and a small number of α-helix appeared,meanwhile,the main secondary structure became random coil.Conclusion The type Ⅱ collagen purified from Prionace glauca was a typical fibrous protein with excellent biochemical characteristics as a potential functional biomaterial." @default.
- W2361443215 created "2016-06-24" @default.
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- W2361443215 date "2013-01-01" @default.
- W2361443215 modified "2023-09-26" @default.
- W2361443215 title "Studies on thermostability,circular dichroism and Infrared spectral characteristics of type II collagen" @default.
- W2361443215 hasPublicationYear "2013" @default.
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