以多孔玻璃为参照，研究吸附在玻璃表面的蛋白质活性降低的情况。

Decreased activity of proteins adsorbed onto glass surfaces with porous glass as a reference.

作者信息

Mizutani T

出版信息

J Pharm Sci. 1980 Mar;69(3):279-82. doi: 10.1002/jps.2600690309.

Abstract

The biological activity of proteins bound to controlled-pore glass surfaces was studied as a model of denaturation of biologicals upon storage in glass containers. After adsorption onto the glass for 1 week, the activities of alkaline phosphatase, catalase, and horse-radish peroxidase recovered from the glass column were 88, 63, and 97%, respectively. However, the phosphatase activity recovered after adsorption for 3 months was 14% of the total activity loaded onto the column, and the activities recovered of peroxidase and catalase were 48 and 2%, respectively. Insulin had almost full activity after adsorption for 3 months, but calcitonin activity was absent. The scission of peptide bonds of proteins eluted after adsorption for 3 months was not observed, but dissociation to the subunits was found. The proteins were active in the state adsorbed onto glass surfaces.

摘要

以结合在可控孔径玻璃表面的蛋白质的生物活性作为生物制品在玻璃容器中储存时变性的模型进行了研究。吸附到玻璃上1周后，从玻璃柱回收的碱性磷酸酶、过氧化氢酶和辣根过氧化物酶的活性分别为88%、63%和97%。然而，吸附3个月后回收的磷酸酶活性为加载到柱上总活性的14%，回收的过氧化物酶和过氧化氢酶活性分别为48%和2%。胰岛素吸附3个月后几乎具有完全活性，但降钙素活性消失。未观察到吸附3个月后洗脱的蛋白质肽键断裂，但发现有亚基解离。这些蛋白质在吸附到玻璃表面的状态下具有活性。