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Refolding Behavior of Urea-Induced Denaturation Collagen

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成果类型:
期刊论文
作者:
Wei, Xu;Zhao, Yanqiu;Zheng, Jingjing;Cao, Qin;Li, Sheng;...
通讯作者:
Xu, Chengzhi(xuchengzhi@whpu.edu.cn);Wang, Haibo(wanghaibo@whpu.edu.cn)
作者机构:
[Xu, Chengzhi; Li, Sheng; Wei, Benmei; Zheng, Jingjing; Wang, Haibo; He, Lang; Wei, Xu; Zhang, Juntao] Wuhan Polytech Univ, Sch Chem & Environm Engn, Wuhan, Hubei, Peoples R China.
[Cao, Qin; Zhao, Yanqiu] Wuhan Polytech Univ, Sch Food Sci & Engn, Wuhan, Hubei, Peoples R China.
通讯机构:
[Chengzhi Xu; Haibo Wang] S
School of Chemistry and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, P. R. China<&wdkj&>School of Chemistry and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, P. R. China
语种:
英文
关键词:
collagen;urea;refolding behavior
期刊:
Macromolecular Research
ISSN:
1598-5032
年:
2021
卷:
29
期:
6
页码:
402-410
基金类别:
National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21676208, 21706201]; Natural Science Foundation of Hubei ProvinceNatural Science Foundation of Hubei Province [2018CFA030, 2019CFB252]; Application Foundation Frontier Project of Wuhan Science and Technology Bureau [2019020701011478]
机构署名:
本校为第一机构
院系归属:
食品科学与工程学院
化学与环境工程学院
摘要:
Exploration of the denaturation and refolding of natural collagen is important for the application of collagen and its denatured products. In this study, using urea as a denaturant, we prepared a denatured natural collagen product and analyzed its structural changes. The denaturation treatment severely destroyed the triple helix conformation of collagen, but had no significant effect on the primary structure of its a chains or the covalent cross-linking between a chains. Next, we observed the refolding behavior of the denatured collagen by remo...

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