共查询到19条相似文献,搜索用时 140 毫秒
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本课题以生皮胶原为研究基质,以H2O2、CLO-、O3、O2为氧化剂,研究氧化剂与胶原作用过程中胶原分子量和胶原氨基酸组成的变化规律、胶原分子中化学基团的变化规律,建立氧化剂与胶原发生化学作用的结构模型;研究氧化剂对胶原的强度、玻璃化温度、耐湿热稳定性、等电点等特性的影响规律。 相似文献
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混合鲨鱼和猪皮的Ⅰ型胶原纤维,其集结、成长的纤维重组过程,较单一的鲨鱼或猪皮Ⅰ型胶原纤维样品重组过程快。重组的混合胶原纤维,对比鲨鱼胶原单独组成的胶原纤维而言,有更强的抗熔解和转化为明胶的能力。混合胶原凝胶的变性温度,比鲨鱼胶原凝胶的变性温度高大约10℃,比猪皮胶原凝胶变忤温度低大约5℃。通过扫描电子显微镜观察.发现混合胶原纤维的直径太小处于鲨鱼和猪皮皎原纤维之间。混合胶原凝胶的比猪皮胶原凝胶的撕裂强度大,比鲨鱼胶原凝胶的撕裂强度小。混合Ⅰ型胶原凝胶的其他物理化学性质处于Ⅰ型鲨鱼胶原凝胶和Ⅰ型猪皮胶原凝胶之间。 相似文献
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本实验以猪皮胶原为研究对象,通过丁二酸酐改性制备了酰化胶原,采用仪器分析法对酰化胶原三股螺旋结构的保留程度进行检测,在此基础上使用原子力显微镜和成纤维细胞培养实验对酰化胶原的生物活性进行了进一步考察。结果表明:胶原的酰化度为62.4%,酰化胶原的等电点降低到4.1。X射线衍射(X-ray diffraction,XRD)、热变性温度、圆二色谱法检测结果显示,丁二酸酐改性整体上并未破坏胶原的三股螺旋结构;酰化胶原在原子力显微镜下呈现了胶原特有的纤维结构,成纤细胞培养实验结果发现酰化胶原可以兼容成纤细胞,并在一定程度上促进成纤细胞的增殖,丁二酰化不会破坏胶原的生物活性结构。 相似文献
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胶原的生物合成过程及其调节 总被引:1,自引:0,他引:1
胶原的生物合成涉及一系列的复杂过程,主要包括胶原基因的转录、翻译、胶原分子的后加工、分泌及聚 集等。本文介绍了胶原的生物合成过程,生物合成中所涉及的酶,胶原分子的结构,聚集态结构,调节胶 原合成的多种因素,并对已确定的18种胶原类型,32种具有遗传特异性的多肽链以及它们在动物体内 的分布作了简要描述。 相似文献
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Salmon released to seawater as different smolt types differed significantly in the total collagen content and the solubility of the collagen present. A 11/2 smolt contained more total collagen than 1/2 and 1 smolt types. Less insoluble collagen and more of the pepsin soluble collagen was generally present in 11/2 smolt type as compared with both 1/2 and 1 types, with the exception of prerigor type 1 salmon. No differences between smolt types in acetic soluble collagen were present. Fish with the higher amount of collagen also had the lowest end pH. Although the bled body weight differed, no correlation between body weight and collagen content or its solubility was found. Fish with higher end pH had lower total collagen and pepsin soluble collagen (r = ‐0.77, P = 0.0001 and r = ‐0.51, P = 0.04, respectively, and more insoluble collagen (r = 0.72, P = 0.002). 相似文献
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本文以骆驼掌为原料,以提取时间、加酶量、乙酸浓度、料液比为实验因素,通过正交试验优化胃蛋白酶提取骆驼掌胶原蛋白工艺,并对所提骆驼掌胶原蛋白进行性能分析。结果表明,骆驼掌胶原蛋白的最佳提取工艺为提取时间48 h、胃蛋白酶加酶量4%、乙酸浓度0.50 mol/L、料液比1:15 g/mL,此条件下提取率为30.33%±0.19%。紫外光谱和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)分析表明,所提胶原蛋白符合I型胶原特征,保持了胶原蛋白的三螺旋结构。与牛蹄胶原蛋白性质比较,发现骆驼掌胶原蛋白的吸湿性和保湿性优于牛蹄胶原蛋白,吸油性弱于后者。 相似文献
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分光光度法测定畜禽骨素中胶原蛋白含量 总被引:1,自引:0,他引:1
本文提供了一种快速、简单、准确、成本低的畜禽骨素中胶原蛋白含量的测定方法。通过热法和酸法提取畜禽骨中胶原蛋白,计算其中胶原蛋白与羟脯氨酸含量的比值,得到不同原料骨的胶原蛋白换算系数:猪骨为6.12-6.17,牛骨为6.77,鸡骨为6.27-6.30,羊骨为6.34-6.35,结果表明水溶性和酸溶性的胶原蛋白换算系数差异不显著(P〉0.05)。根据骨素生产实际情况,选用水溶性胶原蛋白换算系数作为骨素中胶原蛋白测定的换算系数,用分光光度法测定热提骨素中羟脯氨酸含量,乘以对应的胶原蛋白换算系数,得到猪骨素、牛骨素和鸡骨素中胶原蛋白含量分别为9.19%、7.92%、9.78%。该方法测定骨素中胶原蛋白含量的相对标准偏差在0.01-0.03%之间,变异系数在0.44-2.26%之间,平均回收率在99.36-100.44%之间,说明分光光度法适用于骨素中胶原蛋白含量的测定。 相似文献
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Phanat Kittiphattanabawon Soottawat Benjakul Sittichoke Sinthusamran Hideki Kishimura 《International Journal of Food Science & Technology》2015,50(9):1972-1978
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of clown featherback (Chitala ornata) were isolated and characterised. Yields of ASC and PSC were 27.64 and 44.63% (dry weight basis) with total collagen recovery of 82.08%. Both collagens contained glycine as the major amino acid with relatively high content of proline, hydroxyproline and glutamic acid/glutamine. Nevertheless, they had the low content of cysteine, histidine and tryrosine. The collagen was characterised as type I, comprising (α1)2α2‐heterotrimer. Pepsin‐aided process did not affect triple‐helical structure of PSC as determined by FTIR spectra. Thermal transition temperature of ASC (36.28 °C) was slightly higher than that of PSC (35.23 °C). However, no differences in isoelectric point (5.54–5.68) between ASC and PSC were observed. Therefore, collagen from the skin of clown featherback could be successfully extracted for further applications. 相似文献
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Hiroyuki Ijima Ryohei Ogata Yusuke Murasawa Pi-Chao Wang 《Journal of Bioscience and Bioengineering》2010,109(2):179-181
Primary rat hepatocytes were cultured on type V collagen. Hepatocyte spreading on type V collagen was inferior compared with that on type I collagen. However, the albumin production rates of hepatocytes cultured on type V collagen were approximately twice as high as those of hepatocytes cultured on type I collagen. 相似文献
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胶原在组织工程中的应用 总被引:6,自引:0,他引:6
胶原现已被视为最有用途的生物材料。胶原所具有的优越的生物相容性和安全性、生物可降解性和弱抗原性 ,使得它已成为医学应用中最基本的材料。应用于组织工程 ,例如皮肤替换、骨替换以及人造血管和瓣膜的替换 ,就是胶原的重要用途之一。 相似文献
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Kathleen Hofman Kim Bulling Susan Marshall Terry Chadderton 《Journal of the Institute of Brewing》2008,114(3):257-261
Concerns about the potential allergenicity of collagen proteins remaining after beverage fining have necessitated development of methods to detect collagen in beer at very low concentrations. We have developed a semi‐quantitative SDS‐PAGE/densitometer method suitable for use in brewer's laboratories, for detection of residual native collagen at levels as low as 0.03 ppm (depending on the beer). The method is based on the fibril‐forming properties of collagen molecules at elevated ionic strength. It will not detect denatured collagens so cannot be used on pasteurised beers. For a quantitative reference that compensates for significant differences in beer composition, and the different fining agents, a known amount of the acid‐soluble fraction of the fining agent is added to the test beer to set limits of detection for the test. Densitometer results from the SDS‐PAGE gels can vary with sample volume, depending on background interference but this can be reduced by careful selection of gel loading volumes. Fining out of the added collagen occurs in some beers, so less collagen is detected in the reference samples than expected. However, as long as densitometer readings for the sample are below those of the spiked reference, then collagen levels can be declared with confidence as being less than those of the reference. 相似文献