Decreased activity of proteins adsorbed onto glass surfaces with porous glass as a reference.
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.
D000327:Adsorption; D000469:Alkaline Phosphatase; D002116:Calcitonin; D005898:Glass; D007328:Insulin; D008970:Molecular Weight; D010544:Peroxidases; D011489:Protein Denaturation; D011506:Proteins; D013499:Surface Properties
D007328:Insulin; D011506:Proteins; D002116:Calcitonin; D010544:Peroxidases; D000469:Alkaline Phosphatase