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. 2008 Mar 1;94(5):1766–1772. doi: 10.1529/biophysj.107.116590

Figure 2.

Figure 2

(A) Time course of protein expression. Protein expression was induced with 1 mM IPTG at 37°C for the time shown above the SDS-PAGE. Aliquots of bacteria were taken at the indicated intervals and directly loaded on the SDS-PAGE. The proteins were stained with colloidal Coomassie. The position of full-length GADS is shown with an arrow. As seen in the gel, GADS is the major protein present after induction, with an estimated molecular mass of 37 kDa. The protein molecular mass markers used were lysozyme (14 kDa), β-lactoglobulin (18 kDa), restriction endonuclease Bsp981 (25 kDa), carbonic anhydrase (37 kDa), ovalbumin (45 kDa), bovine serum albumin (66 kDa), and β-galactosidase (116 kDa). (B) Size-exclusion chromatography of folded full-length GADS. Elution volumes of the molecular mass standards are indicated with numbered arrows. The standards used were 1), albumin, 67 kDa; 2), ovalbumin, 43 kDa; 3), chymotrypsinogen A, 25 kDa; and 3), ribonuclease A, 14 kDa. Blue Dextran (2000 kDa) was used to measure the void volume of the column. The estimated mass of the full-length GADS (major peak) is 37 kDa.