title: Characterization of a proteolytic enzyme in the skin secretions of Xenopus laevis.
abstract: Enzymes present in the skin secretions of Xenopus laevis were fractionated by ion exchange chromatography. One of the proteases obtained was found to catalyse cleavage on the COOH-side of peptide sequences containing consecutive hydrophobic and basic residues. Evidence is presented that the enzyme is a cysteine protease with an optimum pH of 5.0 to 6.0. The characteristic specificity of this enzyme suggests that it may fulfil a role in propeptide processing.
authors.affiliation: National Institute for Medical Research, Mill Hill, London.
authors.forename: N J
authors.initials: NJ
authors.lastname: Darby
authors.forename: D G
authors.initials: DG
authors.lastname: Smyth
mesh_terms: D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003546:Cysteine Endopeptidases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011480:Protease Inhibitors / Q000494:pharmacology; D012867:Skin / Q000201:enzymology* / Q000378:metabolism; D014982:Xenopus laevis / Q000378:metabolism*
chemical_list: D011480:Protease Inhibitors; D003546:Cysteine Endopeptidases