HEAT-INDUCED AGGREGATION OF EGG-WHITE PROTEINS AS STUDIED BY VERTICAL FLAT-SHEET POLYACRYLAMIDE-GEL ELECTROPHORESIS
HEAT-INDUCED AGGREGATION OF EGG-WHITE PROTEINS AS STUDIED BY VERTICAL FLAT-SHEET POLYACRYLAMIDE-GEL ELECTROPHORESIS
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DOI：
10.1111/j.1365-2621.1981.tb04498.x
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发表时间：
1981-01-01
影响因子：
3.9
通讯作者：
SATO, Y
中科院分区：
文献类型：
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作者：
MATSUDA, T;WATANABE, K;SATO, Y
用垂直平板聚丙烯酰胺凝胶电泳法研究了蛋清中蛋白质的热诱导聚集。蛋清蛋白的分步聚集是由加热引起的。即使加热120min，卵清蛋白和球蛋白A1和A2在70℃时也不能在蛋清中聚集，转铁蛋白和类卵粘蛋白在60℃和76℃时也不能聚集。在热处理条件下，卵黄蛋白抑制物比类卵粘蛋白更不稳定，黄素蛋白在蛋清中热诱导聚集的时间依赖性大于其他蛋白。
Heat‐induced aggregation of proteins in egg white was investigated by a vertical flat‐sheet polyacrylamide gel electrophoretic method. The fractional and step‐wise aggregation of egg white proteins was caused by heating. Even with a heating time of 120 min, ovalbumin and globulins Al and A2 failed to aggregate in egg white (pH 7 and 9) at 70°C, and ovotransferrin and ovomucoid also did not aggregate in egg white at 60°C (pH 9) and 76°C (pH 7 and 9), respectively. The ovoinhibitor was much more unstable than ovomucoid under heat‐treatment, and the time dependency of heat‐induced aggregation of flavoprotein was greater than those of the other proteins in egg white.