V. Walreavens et al., ISOLATION AND PRELIMINARY CHARACTERIZATION OF THE CYSTEINE-PROTEINASES FROM THE LATEX OF CARICA-CANDAMARCENSIS HOOK, Biological chemistry Hoppe-Seyler, 374(7), 1993, pp. 501-506
The cysteine-proteinase chymopapain from Carica papaya L. is used for
chemonucleolysis of damaged human intervertebral spinal discs. The pur
ification 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, pH 5.0. They could be furt
her purified by rechromatography under similar conditions. The isolate
d enzymes have been characterized by PAGE, analysis of the Fourier tra
nsform infrared spectra, preliminary studies of their specificities as
well as a comparison of the N-terminal amino-acid sequences up to pos
ition 43. CC-III proved to be glycosylated. CC-I and CC-III from Caric
a candamarcensis Hook are suggested to correspond to papain and chymop
apain from Carica papaya L., respectively.