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. 2005 Aug 23;390(Pt 2):475–484. doi: 10.1042/BJ20050233

Figure 1. Purification of chLBD extracted from IBs and refolded on a Q-Sepharose column.

Figure 1

The column (2.5 cm×7 cm) was equilibrated with 10 mM Tris/HCl (pH 9.0) at 4 °C. The dialysed solution of refolded protein was applied to the column at a rate of 400 ml/h. Elution was carried out using a discontinuous NaCl gradient in the same buffer at 400 ml/h, and 50 ml fractions were collected. Protein concentration was determined by measuring absorbance at 280 nm. Every third tube was analysed for chLBD content by gel filtration in a Superdex™ 75 HR column. Fractions eluted with 150 mM NaCl (underlined) contained monomeric protein and were pooled.