Skin surface proteolytic activity: Partial characterization and identification

Uri Wormser*, Berta Brodsky, Eldad Victor Moor, Arie Eldad, Rivka Gal, Abraham Nyska, Ron Kohen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Skin surface proteolytic activity in the living animal was determined by a sensitive, non-invasive methodology developed in our laboratory. A non- leaky well was constructed on the shaved back of an anesthetized guinea pig. The well contained the reaction mixture including the substrate 125I-S- carboxymethylated insulin B-chain (ICMI). The proteolytic activity was shown to be time-dependent. The activity was strongly inhibited by pepstatin A, indicating the involvement of aspartic proteinase(s) such as cathepsin D and/or E. Pretreatment of the skin with propylene glycol blocked the proteolytic activity. The present study demonstrates the presence of proteolytic activity located on skin surface using a unique, non-invasive method for in situ proteinase determination in the living animal.

Original languageAmerican English
Pages (from-to)207-212
Number of pages6
JournalAdvances in Experimental Medicine and Biology
StatePublished - 1998


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