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Int J Biol Macromol ; 79: 618-26, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-26026980

RESUMO

Collagen is considered to be one of the most useful biomaterials with different medical applications. However, collagen properties differ from one source to another. The aim of this study was to extract, purify, characterize and perform preliminary biological evaluation of type I collagen from scales of Egyptian Nile Tilapia. Pepsin-solubilized collagen (PSC) was successfully prepared from Nile Tilapia fish scale waste. Lyophilized collagen was dissolved in dilute HCl to form acidic collagen solutions (ACS) which was neutralized to form gel. To confirm the biocompatibility of the produced gel, baby hamster kidney (BHK-21) fibroblast cells were seeded onto a 3D collagen gel (0.3% and 0.5%, w/v). The results of an SDS-PAGE test showed that the extracted collagens were type I collagen, with α chain composition of (α1)2α2. Thermal analysis showed that the denaturation temperature was 32 °C. X-ray diffraction (XRD) analysis and Fourier-transform infrared spectra (FTIR) showed that the extracted collagen had a triple helix structure. Active proliferation of BHK-21 cells with no signs of toxicity was evident with both collagen gel concentrations tested. The results show that Nile Tilapia scales can be an effective source of collagen extraction that could be used as a potential biomaterial in biomedical applications.


Assuntos
Ciclídeos , Colágeno Tipo I/química , Proteínas de Peixes/química , Animais , Materiais Biocompatíveis/química , Adesão Celular , Linhagem Celular , Forma Celular/efeitos dos fármacos , Colágeno Tipo I/farmacologia , Colágeno Tipo I/ultraestrutura , Cricetinae , Meios de Cultura , Proteínas de Peixes/farmacologia , Proteínas de Peixes/ultraestrutura , Géis/química , Géis/farmacologia , Teste de Materiais , Desnaturação Proteica , Espectroscopia de Infravermelho com Transformada de Fourier , Difração de Raios X
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