Chymopapain. Chromatographic purification and immunological characterization
- 1 October 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 223 (1) , 81-88
- https://doi.org/10.1042/bj2230081
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.This publication has 18 references indexed in Scilit:
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