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. 1984 Oct 1;223(1):81–88. doi: 10.1042/bj2230081

Chymopapain. Chromatographic purification and immunological characterization.

D J Buttle, A J Barrett
PMCID: PMC1144267  PMID: 6437389

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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