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. Author manuscript; available in PMC: 2008 May 30.
Published in final edited form as: Free Radic Biol Med. 2006 Jul 15;41(8):1315–1324. doi: 10.1016/j.freeradbiomed.2006.07.014

Fig. 2.

Fig. 2

Reduced nonprotein thiols interact with MMP-9′s active-site Zn2+ molecule. (A) Immunoblot analyses were conducted using the biotinylated GSH analogue, BioGee, to determine the interaction of reduced nonprotein thiols with the active-site Zn molecule. (B) Western blot analyses were then conducted on the same washed membrane to confirm the integrity of the MMP-9 protein. Lane assignments were: (1) active MMP-9 with no incubation, (2) active MMP-9 + vehicle (ethanol) control with no incubation, (3) active MMP-9 + vehicle + 4 h incubation, (4) active MMP-9 + 464 μM (800×) BioGee, (5) active MMP-9 + 464 μM TPEN first, followed by 464 μM BioGee, (6) active MMP-9 + 464 μM BioGee first, followed by 464 μM TPEN, (7) active MMP-9 + 1160 μM (2000×) BioGee, (8) active MMP-9 + 1160 μM TPEN first, followed by 1160 μM BioGee, and (9) active MMP-9 + 1160 μM BioGee first, followed by 1160 μM TPEN.