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首页> 外文期刊>Biochemistry >Effect of alpha-Crystallin on Thermal Aggregation of Glycogen Phosphorylase b from Rabbit Skeletal Muscle
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Effect of alpha-Crystallin on Thermal Aggregation of Glycogen Phosphorylase b from Rabbit Skeletal Muscle

机译：α-结晶蛋白对兔骨骼肌糖原磷酸化酶b热聚集的影响

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Thermal aggregation of rabbit skeletal muscle glycogen phosphorylase b (Phb) has been investigated using dynamic light scattering under conditions of a constant rate of temperature increase (1 K/min). The linear behavior of the dependence of the hydrodynamic radius on temperature for Phb aggregation is consistent with the idea that thermal aggregation of proteins proceeds in the kinetic regime wherein the rate of aggregation is limited by diffusion of the interacting particles (the regime of "diffusion-limited cluster-cluster aggregation"). In the presence of alpha-crystallin, a protein exhibiting chaperone-like activity, the dependence of the hydrodynamic radius on temperature follows the exponential law; this suggests that the aggregation process proceeds in the kinetic regime where the sticking probability for colliding particles becomes lower than unity (the regime of "reaction-limited cluster-cluster aggregation"). Based on analysis of the ratio between the light scattering intensity and the hydrodynamic radius of Phb aggregates, it has been concluded that the addition of alpha-crystallin results in formation of smaller size starting aggregates. The data on differential scanning calorimetry indicate that alpha-crystallin interacts with the intermediates of the unfolding process of the Phi molecule. The proposed scheme of thermal denaturation and aggregation of Phb includes the stage of reversible dissociation of dimers of Phi into monomers, the stage of the formation of the starting aggregates from the denatured monomers of Phb, and the stage of the sticking of the starting aggregates and higher order aggregates. Dissociation of Phi dimer into monomers at elevated temperatures has been confirmed by analytical ultracentrifugation.
机译：在恒定的升温速率（1 K / min）下，利用动态光散射研究了兔骨骼肌糖原磷酸化酶b（Phb）的热聚集。 Phb聚集的流体动力学半径对温度的依赖性的线性行为与这样的想法是一致的，即蛋白质的热聚集是在动力学过程中进行的，在该动力学过程中，聚集的速率受相互作用粒子的扩散限制（“扩散-有限的群集-群集聚合”）。在α-晶状体蛋白（一种表现出类似伴侣的活性的蛋白质）的存在下，流体动力学半径对温度的依赖性遵循指数规律。这表明聚集过程是在动力学方案中进行的，在该动力学方案中，碰撞粒子的粘附概率变得低于统一性（“反应受限的簇-团簇聚集”方案）。根据对Phb聚集体的光散射强度与流体力学半径之间的比率的分析，可以得出结论，添加α-晶状体蛋白会导致形成较小尺寸的起始聚集体。差示扫描量热法的数据表明α-晶状体蛋白与Phi分子展开过程的中间体相互作用。提议的Phb的热变性和聚集方案包括Phi二聚体可逆解离为单体的阶段，由Phb的变性单体形成起始聚集体的阶段以及起始聚集体和Pb的粘附阶段。高阶集合。通过分析超速离心已证实在升高的温度下Phi二聚体解离成单体。

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