Abstract
Cathepsin D is usually assayed by following the release of the trichloroacetic (TCA)-soluble peptides from denatured haemoglobin at 280 nm, but some artefacts may appear giving false results. Cathepsin D activity has therefore been assayed under different conditions in muscle, liver and dry-cured ham extracts. Substantial errors (around 50–56%) become evident when using the classical standard assay. The assay of cathepsin D activity in muscle extracts should include the use of a blank containing a specific inhibitor such as isovalerylpepstatin.
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