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. 2000 Jan 15;28(2):552–559. doi: 10.1093/nar/28.2.552

Figure 1.

Figure 1

Purification and molecular mass determination of the LrpC protein. (A) SDS–PAGE (15%) stained with Coomassie Blue. (B) Western blot of the gel presented in (A) highlighted with polyclonal antibodies raised against EcoLrp. Lane 1, cell lysate (induced cells); lane 2, polyethylenimine supernatant; lane 3, ammonium sulphate (60% saturation) pellet; lane 4, eluate from the phosphocellulose column (400 mM NaCl); lane 5, eluate from the FPLC Superose 12 column (1 M NaCl). The molecular mass standards, in kDa, are indicated. (C) Calibration graph of molecular mass against Kav of several protein standards (filled circle) for a Superose 12 column using the same conditions as described for LrpC (open circle).