Walreavens V, Jaziri M, van Beeumen J, Schnek A G, Kleinschmidt T, Looze Y
Protein Chemistry Unit, Faculty of Medicine, University of Brussels, Belgium.
Biol Chem Hoppe Seyler. 1993 Jul;374(7):501-6. doi: 10.1515/bchm3.1993.374.7-12.501.
The cysteine-proteinase chymopapain from Carica papaya L. is used for chemonucleolysis of damaged human intervertebral spinal discs. The purification of this enzyme is difficult. To overcome these problems, we were looking for a substitute among the cysteine-proteinases of Carica candamarcensis Hook. The latex from unripe fruits was collected in an aqueous solution of methylethanethiolsulfonate to prevent proteolytic activities. The soluble fraction of the lypophilized product provided four enzymatically active peaks (CC-I-CC-IV) during chromatography on CM-Sephadex C-50 in sodium acetate buffer, pH5.0. They could be further purified by rechromatography under similar conditions. The isolated enzymes have been characterized by PAGE, analysis of the Fourier transform infrared spectra, preliminary studies of their specificities as well as a comparison of the N-terminal amino-acid sequences up to position 43. CC-III proved to be glycosylated. CC-I and CC-III from Carica candamarcensis Hook are suggested to correspond to papain and chymopapain from Carica papaya L., respectively.
