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Fig. 1 | Parasites & Vectors

Fig. 1

From: Characterization of a serine protease inhibitor from Trichinella spiralis and its participation in larval invasion of host’s intestinal epithelial cells

Fig. 1

SDS-PAGE analysis of rTsSPI activity for inhibiting trypsin hydrolysis of BSA. a Different quantity of BSA were hydrolyzed by trypsin. Lane M: protein marker; Lane 1: trypsin; Lane 2: BSA; Lanes 3–8: trypsin + BSA (0.75, 1.50, 2.25, 3.00, 3.75 and 4.50 μg, respectively). b Different quantity of rTsSPI were hydrolyzed by trypsin. Lane M: protein marker; Lane 1: trypsin; Lane 2: rTsSPI; Lanes 3–8: trypsin + rTsSPI (3.00, 3.75, 4.50, 5.25, 6.00 and 6.75 μg, respectively). c The trypsin hydrolysis of BSA was inhibited by different quantity of rTsSPI. Lane M: protein marker; Lane 1: trypsin; Lane 2: rTsSPI; Lane 3: BSA; Lanes 4–9: trypsin + BSA + rTsSPI (3.00, 3.75, 4.50, 5.25, 6.00 and 6.75 μg, respectively). d The trypsin hydrolysis of BSA was inhibited by rTsSPI and natural inhibitor PMSF. Lane M: protein marker; Lane 1: TsSPI; Lane 2: BSA; Lane 3: trypsin; Lane 4: trypsin + rTsSPI; Lane 5: trypsin+BSA; Lane 6: rTsSPI+trypsin+BSA; Lane 7: PMSF+trypsin+BSA

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