首页> 外文期刊>Bio/Technology >AGGREGATION OF A LYOPHILIZED PHARMACEUTICAL PROTEIN, RECOMBINANT HUMAN ALBUMIN - EFFECT OF MOISTURE AND STABILIZATION BY EXCIPIENTS
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AGGREGATION OF A LYOPHILIZED PHARMACEUTICAL PROTEIN, RECOMBINANT HUMAN ALBUMIN - EFFECT OF MOISTURE AND STABILIZATION BY EXCIPIENTS

机译:磷脂的蛋白质,重组人白蛋白的聚集-赋形剂对水分和稳定作用的作用。

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摘要

In the presence of water vapor at 37 degrees C, lyophilized recombinant human albumin (rHA) undergoes intermolecular thiol-disulfide interchange, eventually forming high-molecular-weight, water-insoluble aggregates. The relationship between the extent of aggregation and the water content of the lyophilized protein was bell-shaped, with maximum aggregation (over 80% after one day) at approximately 50 g water per 100 g dry protein, corresponding to incubation at 96% relative humidity, Nineteen different excipients were co-lyophilized,vith rHA to test their ability to inhibit aggregation under these conditions. These compounds included low- and high-molecular-weight sugars, as well as various organic acids (amino, hydroxy, and aliphatic), and the simple inorganic salt sodium chloride. Seven of them afforded complete stabilization of rHA against moisture-induced aggregation, The stabilizing potency of the excipients correlated with their water-sorbing capability, presumably due to increasing the moisture level in the vicinity of rHA.
机译:在37摄氏度的水蒸气存在下,冻干的重组人白蛋白(rHA)经历了分子间硫醇-二硫键交换,最终形成了高分子量,水不溶性聚集体。凝集程度与冻干蛋白质水分之间的关​​系呈钟形,最大凝集(一天后超过80%)每100克干蛋白质约有50克水,相当于在96%相对湿度下孵育,通过rHA共冻干19种不同的赋形剂,以测试它们在这些条件下抑制聚集的能力。这些化合物包括低分子量和高分子量糖,以及各种有机酸(氨基,羟基和脂肪族),以及简单的无机盐氯化钠。其中七个提供了rHA对水分诱导的聚集的完全稳定作用。赋形剂的稳定效能与其吸水能力相关,这可能是由于rHA附近的水分含量增加所致。

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