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. 2012 Aug 13;40(19):9717–9737. doi: 10.1093/nar/gks774

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© The Author(s) 2012. 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/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Reduction of p32 results in decreased mitoribosomes. (A) Upper panels: Sedimentation analysis of mitoribosomal particles by centrifugation via a linear 15–30% sucrose density gradient. Fraction numbers are indicated. The migration of mitoribosomal particles in wild-type (+/+), p32-knockout (^−/−) MEFs and p32 re-expressed (^−/−::p32) MEFs was determined by immunoblotting with antibodies against MRPL3 (39S large subunit), MRPS29 (28S small subunit) and p32. Arrows indicate peaks of optical density for the S value markers. Asterisk (*) shows non-specific band of MRPL3 and p32 at top fraction (1–2). (B) Representative blots were analyzed densitometrically. The signal intensity of the protein in each fraction was plotted. The maximum value was 100% for each protein level.

Figure 4. — Reduction of p32 results in decreased mitoribosomes. (A) Upper panels: Sedimentation analysis of mitoribosomal particles by centrifugation via a linear 15–30% sucrose density gradient. Fraction numbers are indicated. The migration of mitoribosomal particles in wild-type (+/+), p32-knockout (^−/−) MEFs and p32 re-expressed (^−/−::p32) MEFs was determined by immunoblotting with antibodies against MRPL3 (39S large subunit), MRPS29 (28S small subunit) and p32. Arrows indicate peaks of optical density for the S value markers. Asterisk (*) shows non-specific band of MRPL3 and p32 at top fraction (1–2). (B) Representative blots were analyzed densitometrically. The signal intensity of the protein in each fraction was plotted. The maximum value was 100% for each protein level.