Fig. 1
From: A human endogenous retrovirus encoded protease potentially cleaves numerous cellular proteins
Purification of HERV-K(HML-2) Protease. A previously established method for purification of prokaryotically expressed HML-2 Pro was employed with minor modifications (see text). Samples were taken at various steps of the procedure, such as bacterial culture before induction (“pre-ind.”), flow-through (“flow-thr.”) after binding of bacterial lysate to Pepstatin A-agarose, two wash fractions, and 4 elution fractions. Proteins were separated by SDS-PAGE in a 15% PAA-gel and visualized by staining with Coomassie Blue. Molecular mass of marker proteins (M) are indicated on the left. Purified, auto-processed HML-2 Pro migrates at approximately 12 kDa