Skin surface proteolytic activity. Partial characterization and identification.

U Wormser; B Brodsky; E V Moor; A Eldad; R Gal; A Nyska; R Kohen

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PubMed · 9561221

Skin surface proteolytic activity. Partial characterization and identification.

U Wormser·B Brodsky·E V Moor·A Eldad·R Gal·A Nyska·R Kohen

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Abstract

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.

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Animals Endopeptidases Guinea Pigs Skin Journal Article

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U Wormser, B Brodsky, E V Moor, A Eldad, R Gal, A Nyska, R Kohen. 1998. Skin surface proteolytic activity. Partial characterization and identification.. https://pubmed.ncbi.nlm.nih.gov/9561221/

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