| Literature DB >> 12489200 |
J Maycock1, S R Wood, S J Brookes, R C Shore, C Robinson, J Kirkham.
Abstract
EMDOGAIN is derived from porcine developing enamel matrix and has been shown to facilitate regeneration of the periodontium, although its mechanism of action is unknown. The aim of the present study was to identify enamel matrix proteins and proteolytic enzymes present in EMDOGAIN and compare them with those extracted from developing porcine enamel itself. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting, and zymography were used to identify the proteins present and to determine their enzyme activity. The results showed that developing enamel contained amelogenins, albumin, amelin, and enamelin. EMDOGAIN, however, contained only amelogenins. Both metalloendoproteases and serine protease activity were revealed in both EMDOGAIN and developing enamel. The roles of the amelogenin and enzyme components, if any, in periodontal regeneration are unknown.Entities:
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Year: 2002 PMID: 12489200 DOI: 10.1080/03008200290000880
Source DB: PubMed Journal: Connect Tissue Res ISSN: 0300-8207 Impact factor: 3.417