Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PROTEASES/pharmacology”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources

Enzymatic debridement of third-degree burns on guinea pigs by Clostridium histolyticum proteinases.

Webster, Marion E. (Walter Reed Army Institute of Research, Washington, D. C.), Patricia L. Altieri, David A. Conklin, Sanford Berman, Joseph P. Lowenthal, and Raymond B. Gochenour. Enzymatic debridement of third-degree burns on guinea pigs by Clostridium histolyticum proteinases. J. Bacteriol. 83:602-608. 1962.-An attempt has been made to correlate in vitro activities of Clostridium histolyticum H-4 proteinases, as measured against azocasein, azocoll, gelatin, and collagen, with their ability to debride full-thickness third-degree burns (360 C, 15 sec) on guinea pigs. The major portion of the debriding activity is tentatively identified as due to the delta-proteinase, in the absence of cysteine, and to a new proteinase contained in the same fraction in the presence of cysteine. Other proteinases produced by this strain were also capable of debriding burns. However, collagenase and the gelatinase of the 0 to 22% fraction did not appear to be essential for the debridement of these burns.Studies of the proteinases produced by this organism have suggested that at least nine and probably more proteolytic enzymes are present. The need for more highly purified proteinases, in order to determine which enzyme(s) is responsible for debridement of guinea pig burns, is evident.

Animals↗