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. 2010 Jun 17;38(19):6803–6812. doi: 10.1093/nar/gkq551

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Cleavage of TAT-fused maize RIP variants by HIV-1 protease. (A) Pro-HIV-MA/CA-16, Pro-HIV-MA/CA-20 and Pro-HIV-MA/CA were cleaved by purified recombinant HIV-1 protease in vitro. Only Pro-HIV-MA/CA was completely cleaved. (B) TAT-Pro-HIV-MA/CA and TAT-Pro-HIV-p2/NC were completely cleaved by HIV-1 protease in vitro. (C) HIV-1_IIIB acutely infected C8166 cells (1 × 10⁶) were incubated with protein samples (0.4 µg in a volume of 2 ml) for 72 h and immunoblotted with anti-MOD polyclonal antibodies specific for Pro-RIP and its cleavage fragments (∼11 and 17 kDa). (D) TAT-Pro-HIV-MA/CA-3aa and TAT-Pro-HIV-MA/CA-2aa were not cleaved by the same in vitro cleavage reaction condition as in (A) and (B). Proteins were resolved by 15% SDS gel.