Identification, characterization, and partial purification of mammalian skin wound hyaluronidase.
A recently described mammalian wound hyaluronidase is successfully characterized and partially purified in the current study. Peak enzyme activity occurred on postwound day 7, pH optimum 4.5. Both crude and purified wound enzyme exhibited endoglycosidic activity against hyaluronate and chondroitin-4-sulfate but not against chondroitin-6-sulfate or dermatan sulfate. A 5.3-fold increase in activity was obtained by the DEAE-Sephadex purification technique described. Polyacrylamide gel electrophoresis yielded a single major band near the gel's midrange and one minor band of lesser electrophoretic mobility. These enzyme characteristics support a biochemical analogy between tissue repair in skin and numerous developmental systems and may also provide a simple means for enzymatic differentiation among chondroitin sulfate isomers.
D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006821:Hyaluronoglucosaminidase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D011817:Rabbits; D012867:Skin / Q000201:enzymology / Q000293:injuries*; D013379:Substrate Specificity; D013997:Time Factors
D006821:Hyaluronoglucosaminidase