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Purification of Murine IgG1 Using UNOsphere S and CHT ,,, Ceramic Hydroxyapatite Chromatography, Rev A

ause the ionic strength of the pooled solution was too high to allow murine IgG1 to bind. The diluted sample was loaded onto the CHT column at 300 cm/hr. Some contaminants were removed by a NaCl gradient. The murine IgG1 was eluted by a phosphate gradient (Figure 3).

The fraction pool was analyzed by SDS-PAGE (Figure 4). We estimated that >95% purity of murine IgG1 was achieved in this purification process.


Process Scale-Up
A 2.2 x 20 cm column was packed with 60 ml of UNOsphere S to a bed height of 16 cm and run as described (Figure 5). Some contaminants were removed, and the murine IgG1 could be isolated in the process at this scale. The results indicated that the UNOsphere S purification process could be scaled up at least 30 times.

The murine IgG1 pool from the UNOsphere S column was further purified by CHT chromatography as described in Figure 6. Murine IgG1 was eluted in a phosphate gradient applied after some contaminants were removed by a NaCl gradient.

SDS-PAGE analysis showed that the scaled-up CHT purification process yields murine IgG1 of similar purity to that in small-scale purification (Figure 7). The murine IgG1 was isolated by phosphate gradient; however, some minor bands were observed in lane 3 when the gel was overloaded with 40 g of a murine IgG1 elution pool. These bands suggest that there are still some degradation products or contaminants in the purified murine IgG1. Average recovery in this scale-up purification process was about 80%. Data from flow cytometry analyses suggests that the murine IgG1 solution from our purification process yields very similar immunospecificit
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