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- W2391915458 abstract "Objective:The development of the next generation of biomaterials for restoration of tissues and organs (i.e., tissue engineering) requires a better understanding of the extracellular matrix.Type I collagen is the major protein in ligament, tendon and skin.The ligament from pig joint is an excellent raw material for the preparation of collagen type I, besides convenient experimental research aspects and benefit to industrial investment (abundant collagen).Interestingly, several ECM components have the ability to form three-dimensional(3D), supermolecular matrices (scaffold) in vitro by a process of self-directed polymerization, self-assembly. It is little know whether the collagen extracted from ligaments can be polymerized into architecture in vitro.Method:we use the acetic acid plus enzymes for depredation the tendon or ligaments, and employ microscopy for analysis of the structural properties, as well as determine the self-assembly properties of purified type I collagen.Results:the type I collagen extracted from the ligaments and tendon.It showed at 116kD and 120kD for α1 chain and α2 chain by gel electrophoresis.The fibrillogenesis of collagen is formed in vitro.Conclusion:we first report that we employ the dark-field microscope for observation of living and analysis of structural properties of collagen fibril.We showed that the formation of fibrils from collagen solution de novo and suggests that supermolecular materials will be employed to bioengineering." @default.
- W2391915458 created "2016-06-24" @default.
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- W2391915458 date "2009-01-01" @default.
- W2391915458 modified "2023-09-24" @default.
- W2391915458 title "Extraction and Purification of Collagen and 3-dimension Characterization of Collagen Fibrillogenesis In Vitro" @default.
- W2391915458 hasPublicationYear "2009" @default.
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