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. Author manuscript; available in PMC: 2011 Mar 1.
Published in final edited form as: Antiviral Res. 2009 Dec 5;85(3):482–489. doi: 10.1016/j.antiviral.2009.12.003

Fig. 2.

Fig. 2

Superdex-200 purification of puromycin-sensitive aminopeptidase from Caco-2 cell homogenates. Active and non-active fractions from the Superdex-200 purification were analyzed by 10% SDS-PAGE, here stained with SYPRO Red. Lanes 4-6 contain active fractions hydrolyzing Val-Ser-cHPMPC, while lanes 2, 3, 7 and 9 are non-active fractions. Lane 8 corresponds to the pooled active MonoQ fractions that were initially applied to the Superdex-200 column. Lanes 1 and 10 are size markers with molecular mass expressed in kDa. The band visible at ∼ 100 kDa in lane 4-6 and 8 was exclusively present in the active fractions and its identity was determined by tandem mass spectrometry and database searches to be puromycin-sensitive aminopeptidase (APP-S).