Ability of alphas-Casein to suppress the heat aggregation of ovotransferrin.
Ability of alphas-Casein to suppress the heat aggregation of ovotransferrin.
复制标题
α-酪蛋白抑制卵转铁蛋白热聚集的能力。
DOI：
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复制
发表时间：
2004
影响因子：
6.1
通讯作者：
Hiromi Moriwaki
中科院分区：
文献类型：
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作者：
N. Matsudomi;Y. Kanda;Y. Yoshika;Hiromi Moriwaki
通过在10 mM磷酸盐缓冲液（pH 7.0）中于80 ℃加热20 min，研究了酪蛋白对卵转铁蛋白（OT）热聚集的影响。用浊度显色法和聚丙烯酰胺凝胶电泳法研究了酪蛋白与OT的热相互作用。结果表明，酪蛋白能有效地抑制热不稳定OT的热诱导聚集。NaCl的存在下，对加热的抑制能力降低的拟南芥-酪蛋白。脱磷酸化的酪蛋白对OT聚集的抑制作用弱于天然酪蛋白。我们的研究结果表明，酪蛋白与热变性OT通过其暴露的疏水表面和磷酸丝氨酸残基相互作用。这种相互作用似乎是重要的，有助于抑制聚集的加热OT。酪蛋白对OT热聚集的抑制作用部分归因于酪蛋白的加入使白色蛋白形成透明凝胶。
The effects of alphas-casein on heat aggregation of ovotransferrin (OT) were studied by heating at 80 degrees C for 20 min in 10 mM phosphate buffer, pH 7.0. The heat interactions between alphas-casein and OT were followed by turbidity development and polyacrylamide gel electrophoresis. We found that alphas-casein can effectively suppress the heat-induced aggregation of heat-labile OT. The suppressive ability of alphas-casein was reduced by the presence of NaCl on heating. Dephosphorylated alphas-casein had less ability to suppress the aggregation of OT than native alphas-casein. Our results indicate that alphas-casein interacts with the heat-denatured OT through its exposed hydrophobic surface and phosphoserine residue. Such interactions seem to be important in helping to suppress the aggregation of heated OT. The suppressive effects of alphas-casein on heat aggregation of OT would be partially ascribed to the formation of transparent gel from egg white by the addition of alphas-casein.