The server is under maintenance between 08:00 to 12:00 (GMT+08:00), and please visit later.
We apologize for any inconvenience caused
Login  | Sign Up  |  Oriprobe Inc. Feed
China/Asia On Demand
Journal Articles
Bookmark and Share
Study on isolation,purification and identification of collagen type Ⅱ from porcine articular cartilage
Pages: 389-391
Year: Issue:  5
Journal: Journal of Zhenjiang Medical College

Keyword:  collagen type Ⅱrheumatoid arthritiscartilageproteoglycan;
Abstract: Objective: To isolate and purify collagen type Ⅱ(CⅡ) from porcine articular cartilage and identify its purity.Methods: The porcine articular cartilage was selected as raw material.Guanidine hydrochloride was used to remove the proteoglycans.The digestion of pepsin,salting of sodium chloride,treatment with DE22 cellulose were studied for extracting CⅡ.The purity identification was made by SDS-PAGE,absorption spectrum and amino acid analysis. Results: The proteoglycans could be efficiently removed by 4 mol/L guanidine hydrochloride.The better results were obtained by limited enzyme digestion of pepsin added by two steps.The optimizing concentration of sodium chloride for salting CⅡ was 2.4 mol/L.It was found that the bands of purified CⅡand Sigma CⅡ were at the same location by SDS-PAGE.The absorption peak was at 230 nm.The concentrations of GLY,PRO and ALA were highest by amino acid analysis. Conclusion: The results suggest that the CⅡ isolated from porcine articular cartilage has high purity and accords with the characteristics of collagen type Ⅱ.The improved method we adopted has significant advantages such as simple working process,convenient source of raw material and result reliability.
Related Articles
No related articles found