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.
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