Chymopapain. Chromatographic purification and immunological characterization.
Chymopapain (EC 3.4.22.6) was purified from commercially available spray-dried latex of papaya (Carica papaya) fruit by (NH4)2SO4 fractionation and fast protein chromatography on the Mono S cation-exchange column. Multiple forms of chymopapain separated chromatographically were shown to be immunologically identical. A major form was isolated and found to be homogeneous by several criteria, and fully active, and its N-terminal amino acid was identified as tyrosine. Latex from fresh unripe papaya fruit contained predominantly one form of chymopapain, and it is concluded that chymopapain is a single enzyme distinct from the other cysteine proteinases of C. papaya latex.
D000596:Amino Acids / Q000032:analysis; D002852:Chromatography, Ion Exchange; D002917:Chymopapain / Q000276:immunology / Q000302:isolation & purification; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification; D005779:Immunodiffusion
D000596:Amino Acids; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002917:Chymopapain