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SDS-PAGE analysis of amelogenin (AMG) and gelatin samples crosslinked with glutaraldehyde. The samples have been crosslinked for 0, 5, 30 minutes, and 2 h. Crosslinking of amelogenin in the presence of gelatin does not alter the size of the amelogenin multimers, compared to crosslinking in the absence of gelatin. This indicates that only a minor portion of the amelogenin molecules are covalently linked with gelatin during the glutaraldehyde crosslinking reaction.
