The molecular nature of collagen which is synthesized and degraded as a consequence of surgically wounding rat palatal mucosa will be investigated. The soluble (salt) and insoluble (urea, 60 degrees) collagens as well as their subunit composition will be examined. Fractionation of subunits will be accomplished by ion exchange, gel filtration and gel electrophoresis. In addition, interaction of any these collagen subunits with glycoproteins will be examined. Association with carbohydrate-containing proteins will be indicated by the presence of critical markers (sialic acid and glucosamine). Glycoproteins released from a presumed complex by bacterial collagenase digestion will be further characterized. The study will include isotopic labeling of collagen (hydroxyproline) and glycoprotein (sialic acid and glucosamine). This will enhance the sensitivity of detection and provide insight into the dynamics of synthesis and degradation. The objectives are: to gain knowledge of the loss and concomitant replacement of collagen during wound healing of an oral tissue, and to illustrate the dependence of collagen maturation upon association with glycoprotein. A study of wound healing of oral tissues is important per se and as a model system for subsequent examination of the mechanism of host resistance in periodontal disease.