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Extraction And Characterization Of Collagen From Different Biological Tissues

机译:不同生物组织胶原蛋白的提取与表征

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Because many suitable properties, collagen type I is used in medical and cosmetical applications, for this, the collagen extraction from biological tissues as the first source for obtaining this protein is important. We used skin and tail tendon from bovine, and rat tail tendon to obtain collagen type I. Acetic acid was employed to dissolve the collagen from biological tissues, once obtained was characterized using Sodium Dodecyl Sulfate Polyacrilamide Gel Electrophoresis (SDS-PAGE) technique, DSC and SEM. It was found that indeed the collagen type I was obtained. The thermal analysis showed that the denaturation temperature (T_d) was 70°C for all cases and that the folding of the protein at this temperature is irreversible, involving in all cases two steps: an unfolding of the native protein (N) and an irreversible alteration of the unfolded protein (U) to yield a final state (F) that is unable to fold back to the native state. The protein morphology was studied using SEM, it was found that morphology protein is fibrillar. The results suggested that the obtaining process is very efficient because the collagen concentration obtained was very high.
机译:由于许多合适的性质,胶原型I用于医疗和美容应用中,因此,作为获得该蛋白质的第一源的生物组织提取胶原蛋白是重要的。我们使用从牛的皮肤和尾肌腱,大鼠尾肌腱获得胶原型I.用硫酸钠硫酸钠聚酰胺凝胶电泳(SDS-PAGE)技术,DSC的表征乙酸溶解胶原蛋白。乙酸从生物组织中溶解胶原蛋白。和sem。结果发现,实际上是我获得的胶原蛋白类型。热分析表明,所有病例的变性温度(T_D)为70℃,并且蛋白质在该温度下的折叠是不可逆转的,涉及所有情况下的两个步骤:天然蛋白质(n)的展开和不可逆转的展开展开蛋白质(U)的改变产生最终状态(f),无法折回原生状态。使用SEM研究了蛋白质形态,发现形态蛋白质是纤维状。结果表明,获得过程非常有效,因为获得的胶原浓度非常高。

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