Extraction And Structural Characterization Of Bovine Bone Type I Collagen
Keywords
Bovine Bone, Type ¢ñ Collagen, Extraction, Sds-Page Electrophoresis, Differential Scanning Calorimetry (Dsc), Fourier Transform Infrared Spectroscopy
Abstract
The extraction process (degreasing, decalcification, extraction medium) and structural characterization of bovine bone collagen were studied. The results showed that the optimal extraction process conditions were: low-temperature reflux degreasing with ether, decalcification with 0.48% hydrochloric acid, bone particle size of 5 mm ¡Á 10 mm, and a compound of 1% citric acid and 1% pepsin as the extraction medium. The purified bovine bone collagen was measured by UV scanning analysis, FT-IR, DSC heat shrinkage temperature and SDS-PAGE gel electrophoresis, and compared with the standard bovine tendon type I collagen, and it was determined that the proposed protein was a typical type I Collagen is electrophoretically pure and well maintains the 3-stranded helical structure of type I collagen.
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Original research was done by Liu Lili, Yang Xieli, Ma Meihu
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