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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Effect of a-crystallin on thermostability of mitochondrial aspartate aminotransferase
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Effect of a-crystallin on thermostability of mitochondrial aspartate aminotransferase

机译:a-结晶蛋白对线粒体天冬氨酸转氨酶热稳定性的影响

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摘要

Effect of a-crystallin on thermal inactivation, denaturation and aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has been in the focus of this study. Acceleration of heat-induced inactivation of mAAT was demonstrated in the.presence of a-crystallin. According to the data of differential scanning calorimetry, α-crystallin induces destabilization of the mAAT molecule. The size of protein aggregates formed at heating of mAAT at a constant rate (1 °C/min) has been defined by dynamic light scattering. The obtained data show that aggregation of mAAT in the presence of a-crystallin proceeds in the regime of reaction-limited cluster-cluster aggregation.
机译:α-晶状体蛋白对猪心脏线粒体(mAAT)的天冬氨酸氨基转移酶的热失活,变性和聚集的影响一直是本研究的重点。 α-晶状体蛋白的存在证明了热诱导的mAAT失活的加速。根据差示扫描量热法的数据,α-晶状体蛋白诱导mAAT分子的不稳定。通过动态光散射确定了在以恒定速率(1°C / min)加热mAAT时形成的蛋白质聚集体的大小。所获得的数据表明,在α-晶状体蛋白存在下,mAAT的聚集以反应受限的簇-簇聚集的方式进行。

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