Fig. 9: SDS-PAGE analysis of the untreated and proteolytic enzyme-treated AAV capsids.
From: Adeno-associated virus serotype 2 capsids with proteolytic cuts by trypsin remain intact and potent
A Comparison of the trypsin digestion of the modified and the wild-type AAV2 capsids. Untreated AAV2 capsids as control (C); Trypsin-treated AAV2 capsids (T). The red arrows indicate the major fragments. B Proteolytic digestion of AAV9 capsids. Lane 1: marker; lane 2: untreated AAV9 capsids as control (C); lane 3: trypsin-treated AAV9 capsids; lane 4: CatD-treated AAV9 capsids; lane 5: CatL-treated AAV9 capsids; lane 6: CatB-treated AAV9 capsids; lane 7: chymotrypsin-treated AAV9 capsids; lane 8: Asp-N-treated AAV9 capsids; lane 9: pepsin-treated AAV9 capsids. C Proteolytic digestion of AAV5 and AAV8 capsids. Lane 1: marker; lane 2: untreated AAV5 capsids as control (C); lane 3: trypsin-treated AAV5 capsids; lane 4: CatD-treated AAV5 capsids; lane 5: CatL-treated AAV5 capsids; lane 6: chymotrypsin-treated AAV5 capsids; lane 7: chymotrypsin only; lane 8: untreated AAV8 capsids as control (C); lane 9: trypsin-treated AAV8 capsids; lane 10: CatD-treated AAV8 capsids; lane 11: CatL-treated AAV8 capsids; lane 12: chymotrypsin-treated AAV8 capsids.
