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The cysteine proteinases of the pineapple plant.

The Biochemical journal (1990-03-15)
A D Rowan, D J Buttle, A J Barrett
RÉSUMÉ

The pineapple plant (Ananas comosus) was shown to contain at least four distinct cysteine proteinases, which were purified by a procedure involving active-site-directed affinity chromatography. The major proteinase present in extracts of plant stem was stem bromelain, whilst fruit bromelain was the major proteinase in the fruit. Two additional cysteine proteinases were detected only in the stem: these were ananain and a previously undescribed enzyme that we have called comosain. Stem bromelain, fruit bromelain and ananain were shown to be immunologically distinct. Enzymic characterization revealed differences in both substrate-specificities and inhibition profiles. A study of the cysteine proteinase derived from the related bromeliad Bromelia pinguin (pinguinain) indicated that in many respects it was similar to fruit bromelain, although it was found to be immunologically distinct.

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Sigma-Aldrich
Bromélaïne from pineapple stem, ≥3 units/mg protein
Sigma-Aldrich
Bromélaïne from pineapple stem, ≥4 units/mg protein, (chromatography purified)