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See Latest ArticlesComparative properties of recombinant human and bovine matrix metalloproteinase-20
Archives of Oral Biology, 06/27/08
Tanimoto LZK et al. - Both proteases were activated by autocatalysis in a similar pattern of fragmentation. Dynamically, rbMMP-20 autoactivated faster and digested a fluorescence-quenched peptide Mca-PLGL-Dpa-AR, a non-amelogenin substrate, more efficiently than rhMMP-20. However, rhMMP-20 showed higher enzymatic activity for a human amelogenin substrate and in addition, it created an extra cleavage site at its C-terminus.
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