Abstract
Commercial pineapple stem acetone powder is a rich source of an unusually complex mixture of proteases (bromelains) and their polypeptide inhibitors. Because of the great multiplicity both of proteolytic enzymes and of their peptide inhibitors in the same biological source, the purification and characterization of individual components are challenging undertakings even by present-day technology. The multiplicity of these proteins has been shown to be a consequence of genetic substitutions in the polypeptide chains, limited proteolysis, partial deamidation, variable content of carbohydrate, and partial cyclization of an amino terminal residue. This article describes procedures for the purification and assay of the bromelain inhibitors and for the isolation of an enzymologically pure bromelain required for assay of the inhibitors. It also discusses the results of recent covalent structural studies of inhibitor VII in which the chemical basis of the microheterogeneity is documented.
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