Physicochemical properties and molecular weight characterisation of porcine dermal collagen digested under varying conditions with clostridium histolytic collagenase

被引：0

作者：

Yeh J.-T. ^{[1
,2
,3
]}

Chang H.-J. ^{[1
]}

Xiao L.-F. ^{[3
]}

Yang L. ^{[3
]}

Zhu P. ^{[2
]}

Huang G.-X. ^{[4
]}

Yao W.-H. ^{[5
]}

机构：

[1] Graduate School of Polymer Engineering, National Taiwan University of Science and Technology, Taipei, P. O. Box

[2] Laboratory of Green Processing and Functional Textiles of New Textile Materials, Wuhan University of Science and Engineering, Ministry of Education, Wuhan

[3] Faculty of Chemistry and Material Science, Hubei University, Wuhan

[4] Department of Polymer Materials, Kun Shan University, Yung Kang, Tainan

[5] Department of Materials and Textiles, Oriental Institute of Technology, Taipei

来源：

E-Polymers | 2010年

关键词：

Compendex;

D O I：

10.1515/epoly.2010.10.1.1226

中图分类号：

学科分类号：

摘要：

Porcine dermal collagen is successfully digested by clostridium histolyticun collagenases (CHC) at varying compositions and conditions. Collagen fragments thus prepared, with significantly low molecular weight but visible denaturation temperatures and/or triple helix structures, may be useful for clinical applications. As evidenced by Sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC) analyses, relatively high molecular weights of α1, α2 subunit, β1, β2dimmers and γ trimmers of the collagen fragments gradually disappear as their incubation temperature and/or time values increase. The time values corresponding to the disappearance of sigmoid plots in the denaturation curves, denaturation endotherm in DSC thermograms and γ bands in SDS-PAGE patterns of digested collagen specimens are the same and reduce significantly as their incubation temperatures increase. Fourier transform infra-red analyses results suggest that the percentages of preserved triple helix structures present in collagen molecules of digested collagen specimens also reduce significantly with increasing the incubation temperature and time values. Possible reasons accounting for the degradation, denaturation and physicochemical properties of digested porcine dermal collagens are explored in this study.

引用

共 33 条

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