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作 者:宋彩丽 尹淑琴[1] 张晓红 常泓 Song Caili;Yin Shuqin;Zhang Xiaohong;Chang Hong(College of Life Sciences, Shanxi Agricultural University, Taigu 030801, China;Periodical Press of Shanxi Agricultural University, Taigu 030801, China)
机构地区:[1]山西农业大学生命科学学院,山西太谷030801 [2]山西农业大学期刊社,山西太谷030801
出 处:《山西农业大学学报(自然科学版)》2020年第2期79-86,共8页Journal of Shanxi Agricultural University(Natural Science Edition)
基 金:国家自然科学基金(31201347)。
摘 要:[目的]探究钙蛋白酶激活蛋白UK114对钙蛋白酶(calpain-1)及钙蛋白酶抑制蛋白(calpastatin)介导的牛肉宰后僵直、成熟过程中肌原纤维蛋白性质的影响。[方法]以calpain-1、calpastatin、重组UK114蛋白处理的牛肉为研究对象,测定牛肉宰后成熟过程中calpain-1的活性变化及肌原纤维蛋白水合特性、小片化指数(MFI)、降解情况等指标的变化规律。[结果]随着孵育时间的延长,肌原纤维蛋白表面疏水性呈先上升后下降趋势,溶解性呈现先下降后升高的趋势;Calpain-1和UK114+calpain-1处理组疏水性和溶解性的极值点分别提前到48 h和24 h;calpastatin处理组疏水性和溶解性的极值点推迟到120 h;但UK114+calpastatin处理组在48 h达到极值点。[结论]UK114蛋白可抑制calpastatin的抑制作用,促进calpain-1对肌原纤维蛋白的降解。[Objective]The purpose of this study was to investigate the effect of calpain activating protein UK114 on the characteristics of myofibrillar mediated by calpain and calpastatin in post-slaughter beef.[Methods]Beef treated with calpain-1,calpastatin,and recombinant UK114 protein was used as the research object.The activity of calpain-1 and the hydration characteristics of myofibrillar protein,the fragmentation index(MFI),and the degradation of myofibrillar protein were measured during the ripening process of beef after slaughter.[Results]With the extension of incubation time,the hydrophobicity of protein surface was increased firstly and then decreased,and the solubility displayed an opposite trend.The greatest values of hydrophobicity and solubility of calpain and UK114+calpain were advanced to 48 h and 24 h post treatment,respectively.The peaks of hydrophobicity and solubility of calpastatin treatment group was delayed to 120 h post treatment;however,the greatest value of UK114+calpastatin treatment group reached the peak point at 48 h.[Conclusion]UK114 protein can suppress the inhibitory effect of calpastatin and promote the degradation of myofibrillar protein by calpain-1.
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