Figure 7
From: Characterization of a core fragment of the rhesus monkey TRIM5α protein
Crosslinking analysis of the LLER protein. A. The LLER protein, purified by nickel-affinity and anion-exchange chromatography, was incubated with the indicated concentrations (in mM) of glutaraldehyde (GA). The protein was then boiled in Laemmli buffer and analyzed on a 4-12% SDS-polyacrylamide gel. The arrow indicates the positions of the monomers (M), dimers (D) and higher-order oligomers (H-O). B. The peak 1 (P1) and peak 2 (P2) fractions of the LLER protein were purified by gel-filtration chromatography and separately crosslinked by incubation with the indicated concentrations of glutaraldehyde (GA). The proteins were then analyzed on a 4-12% SDS-polyacrylamide gel. C, D. The LLER protein was either untreated (C) or crosslinked with glutaraldehyde (D) prior to MALDI-TOF analysis. The molecular mass estimations in daltons for the single mass ionization peaks are shown.