Pepsin digests of human post-burn wound tissues grafted with autologous fresh skin showed a significantly lower ratio, 0.37 +/- 0.04 (mean +/- S.D.), of type III to type I collagen determined by interrupted gel electrophoresis than the ratio, 0.55 +/- 0.13, measured in ungrafted wound tissues (p less than 0.001). In wounds grafted with frozen skin there was no significant difference from ungrafted wounds, but a significantly higher ratio, 0.46 +/- 0.08, than that in wounds grafted with fresh skin (p less than 0.001). These results were consistent with the histological features of the wound tissues.
bovine dental pulp/collagen/pepsin solubilization/CNBr peptide/ developmental change Dental pulp is an unique tissue almost completely enclosed in a calcified tissue, dentine, and its function is specialized for the formation and subsequent maintenance of the dentine. We have already reported that the collagen concentration is fairly low in young bovine third premolar pulps-about 9 per cent by dry weight of pulp at the partly-formed crown stage-but that it increases consistently up to more than 25 per cent at the attrition stage as the pulp matures1). Limited proteolysis with pepsin has been widely employed to solubilize both interstitial and basement-membrane collagens. However, the recovery of pepsin-solubilized collagen is not always satisfactory and is usually frustratingly low. Furthermore , it has been suggested that type III collagen may be more susceptible to pepsin degrada-tion2). In this communication we report on developmental changes in collagen susceptibility to pepsin digestion in bovine dental pulps and compare the relative amount of type I and type III collagens in both pepsin-treated and untreated bovine dental pulp tissues .
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