Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin
Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin
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DOI：
10.1016/j.bpc.2009.11.002
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发表时间：
2010-02-01
影响因子：
3.8
通讯作者：
Kurganov, Boris I.
中科院分区：
文献类型：
--
作者：
Bumagina, Zoya M.;Gurvits, Bella Ya.;Kurganov, Boris I.
用动态光散射技术研究了二硫苏糖醇（DTT）诱导牛乳中α-乳白蛋白聚集的动力学。对加入DTT后在α-乳白蛋白溶液中形成的颗粒按尺寸分布的分析表明，聚集过程的初始阶段是形成流体动力学半径（R-h）为80-100 nm的起始聚集体的阶段。由于起始聚集体的粘附，蛋白质聚集体的进一步生长继续进行。α-晶状体蛋白对α-乳白蛋白聚集的抑制主要是由于聚集动力学曲线上滞后期持续时间的增加。假设最初形成的未折叠的α-乳白蛋白与α-晶状体蛋白的复合物由于变性蛋白质分子在α-晶状体蛋白颗粒表面上的重新分布而转化为易于聚集的初级簇。(C)2009爱思唯尔有限公司版权所有。
The kinetics of dithiothreitol (DTT)-induced aggregation of alpha-lactalbumin from bovine milk has been studied using dynamic light-scattering technique. Analysis of the distribution of the particles formed in the solution of alpha-lactalbumin after the addition of DTT by size showed that the initial stage of the aggregation process was the stage of formation of the start aggregates with the hydrodynamic radius (R-h) of 80-100 nm. Further growth of the protein aggregates proceeds as a result of sticking of the start aggregates. Suppression of alpha-lactalbumin aggregation by alpha-crystallin is mainly due to the increase in the duration of the lag period on the kinetic curves of aggregation. It is assumed that the initially formed complexes of unfolded alpha-lactalbumin with alpha-crystallin were transformed to the primary clusters prone to aggregation as a result of the redistribution of the denatured protein molecules on the surface of the alpha-crystallin particles. (C) 2009 Elsevier B.V. All rights reserved.