Extraction, Purification And Identification Of Type Ii Collagen From Sheep Cartilage
Keywords
Type Ii Collagen, Cartilage, Proteoglycans
Abstract
Objective To extract and purify type II collagen from sheep costal cartilage and identify it. Methods Sheep costal cartilage was selected as the raw material, and after degreasing and decalcification, proteoglycans were removed with guanidine hydrochloride, and the protein was extracted and purified through pepsin digestion, sodium chloride salting out and other steps, and then identified. Results: 4mol/L guanidine hydrochloride can effectively remove proteoglycans, and the restriction enzymatic hydrolysis results with pepsin are satisfactory; the best sodium chloride salting-out concentration is 3mol/L. SDS-PAGE electrophoresis results showed that the extracted and purified protein was consistent with type II collagen from Sigma Company. The maximum absorption peak of type II collagen is 212nm. Conclusion Type II collagen extracted from sheep costal cartilage has high purity and conforms to the characteristics of type II collagen.
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Original research was done by Xiao Xu, Shi Wenda, Yao Qing, Chen Hu, Wang Jiyun, Li Xiaobing, Gao Ling
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