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Assessment of Enamelysin (MMP-20) Selectivity to Three Peptide Bonds on Amelogenin Sequence

Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, 2250 Alcazar Street, Los Angeles, CA 90033, USA;

View larger version (25K): [in a new window]   Figure 1. Typical reverse-phase HPLC profiles of hydrolysis of the 3 synthetic deca-peptides WPA, GWL, and FSM by enamelysin, from zero to 24 hrs.

View larger version (21K): [in a new window]   Figure 2. Comparative cleavage rates of the 3 deca-peptides — FSM , GWL •, and WPA — by recombinant pig enamelysin (rpMMP-20). The rates, which are represented as the ratio of substrate at time t to substrate at time zero (St/S0) as a function of time, are exponential. The data presented in the curve are the means and standard deviations of from 3 to 8 determinations (except 5 hrs of FSM, 8 hrs of GWL, and 12 hrs of FSM, GWL, and WPA, each of which represents one determination). Statistical analysis (two-way ANOVA) revealed no significant difference among the rates of hydrolysis of the 3 peptide bonds by rpMMP-20. Cells had unequal sample sizes (n = 3-8). F = 2.27 (P > 0.10) for the differences among the peptides regardless of time, and F = 84.86 (P < 0.001) for the differences among times regardless of peptide.