Preliminary Evaluation of Vibriolysin, a Novel Proteolytic Enzyme Composition Suitable for the Debridement of Burn Wound Eschar
| Autor: | Don R. Durham, Lillian B. Nanney, Donald Zane Fortney |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Vibriolysin
Swine Administration Topical medicine.medical_treatment Eschar Fibrin Microbiology Bacterial Proteins Drug Stability In vivo medicine Animals General Nursing Protease Debridement biology business.industry Hydrolysis Rehabilitation Proteolytic enzymes Metalloendopeptidases General Health Professions Emergency Medicine biology.protein Surgery medicine.symptom Burns business Elastin |
| Zdroj: | Journal of Burn Care & Rehabilitation. 14:544-551 |
| ISSN: | 0273-8481 |
| DOI: | 10.1097/00004630-199309000-00009 |
| Popis: | Vibriolysin, a proteolytic enzyme secreted by the marine microorganism Vibrio proteolytictts, was evaluated for its efficacy as an enzymatic debridement agent. Initial in vitro experiments revealed that the protease readily hydrolyzed protcinaceous components of eschar (e.g., fibrin, elastin, and in particular, collagen). Enzyme selectivity towards the digestion of denatured proteins but not viable elements was demonstrated in vitro and in vivo by treatment of full-thickness burn wounds with a porcine model. The full-thickness wound eschar was rapidly hydrolyzed by a hydrophilic vibriolysin composition with a resultant wound bed that appeared pink and viable. Vibriolysin exhibited desirable properties heretofore not described for the enzymatic debridement agents, in particular, its selective hydrolysis of dead but not viable tissue, debridement in the absence of bleeding, compatibility with adjunct therapies, and its unique shelf-life stability in a hydrophilic composition at ambient temperature. (J Burn Care Rehabil 1993;14:544-51) |
| Databáze: | OpenAIRE |
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