HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences >
Peer-reviewed Journal Articles, etc >

Properties of collagen extracted from Amur sturgeon Acipenser schrenckii and assessment of collagen fibrils in vitro

This item is licensed under:Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International

Files in This Item:
Zhang et al_Texts_tables_figures_highlights.pdf1.53 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79240

Title: Properties of collagen extracted from Amur sturgeon Acipenser schrenckii and assessment of collagen fibrils in vitro
Authors: Zhang, Xi Browse this author
Adachi, Shinji Browse this author →KAKEN DB
Ura, Kazuhiro Browse this author →KAKEN DB
Takagi, Yasuaki Browse this author →KAKEN DB
Keywords: Biochemical characteristics
Collagen fibril
Gene
Issue Date: 15-Sep-2019
Publisher: Elsevier
Journal Title: International Journal of Biological Macromolecules
Volume: 137
Start Page: 809
End Page: 820
Publisher DOI: 10.1016/j.ijbiomac.2019.07.021
Abstract: The objective of this study was to assess the nature of the collagens from the Amur sturgeon to determine its possibility as a potential collagen source for biomedical applications. From a sturgeon (1.22 kg), 6.0 g (dry wt) of skin collagen (SC), 4.1 g of swim bladder collagen (SBC), and 0.4 g of notochord collagen (NC) were obtained. SC and SBC were characterized as type I, and NC as type II collagen. Denaturation temperatures of SC, SBC, and NC were calculated as 28.5, 30.5, and 33.5 °C, respectively. Gene expression of the type I procollagen α2 chain of Amur sturgeon (ascol1a2) was specifically higher than ascol1a1 expression in the swim bladder, suggesting a unique composition of α chains in this organ. SC and SBC had better abilities of fibril formation with unique higher-order structures compared with porcine type I collagen. The maximum transition temperature (Tm) of reassembled fibrils formed in a buffer solution containing NaCl at 0 and 140 mM was 34.4 °C and 38.9 °C in SC, and 40.1 °C and 40.7 °C in SBC, respectively. These characteristic features suggested that sturgeon collagens could be used in the biomedical industries in future applications.
Rights: © 2019. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
https://creativecommons.org/licenses/by-nc-nd/4.0/
Type: article (author version)
URI: http://hdl.handle.net/2115/79240
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 都木 靖彰

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University