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. Author manuscript; available in PMC: 2012 Aug 26.
Published in final edited form as: Arch Oral Biol. 2011 Apr;56(4):331–336. doi: 10.1016/j.archoralbio.2010.10.017

Fig. 1. Comparisons of apatite bindings of rh174 and p.P70T amelogenins by protein assay and SDS-PAGE.

Fig. 1

(A) The saturated amounts of rh174 amelogenin and p.P70T mutant bound to HAP were 875.155 ± 37.083 and 1194.067 ± 32.328 μg/m2 respectively, showing a significant difference in apatite binding between these two types of amelogenins (*P < 0.01). (B) Time curves of adsorption of rh174 amelogenin and p.P70T mutant to CHAP. More than 75% of both rh174 and p.P70T amelogenins bound to CHAP in initial 5 minutes of the binding reactions. The bindings of these amelogenins to CHAP reached their plateaus after 15 minutes of incubation. The binding amounts showed significant differences (*P<0.01) at all time points after 5-minute incubation. (C) The SDS-PAGE revealed that more p.P70T mutated amelogenin was bound to HAP, leaving less protein in the supernatants. Lane 1, rh174 amelogenin control without CHAP; Lane 2, p.P70T mutated amelogenin control without CHAP; Lane 3, rh174 amelogenin remained in supernatant after binding; Lane 4, p.P70Tmutated amelogenin remained in supernatant after binding; Lane 5, rh174 amelogenin bound on CHAP; Lane 6, p.P70Tmutated amelogenin bound on CHAP.