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.1984 Feb;3(2):287-91.
doi: 10.3109/02713688408997211.

Dipeptidyl peptidase III of human cataractous lenses. Partial purification

Dipeptidyl peptidase III of human cataractous lenses. Partial purification

A A Swanson et al. Curr Eye Res.1984 Feb.

Abstract

A partial purification of dipeptidyl peptidase III has been achieved from human cataractous lens. The specific activity was increased 45.5-fold over that of the original aqueous extract. The exopeptidase exhibited a marked preference for the release of Arg-Arg from Arg-Arg-2-NNap at the optimum pH 8.8 and 37 degrees. The Km for this substrate was estimated to be 6.061 X 10(-3). Lens DPP III was inhibited by EDTA, p-chloromercuriphenyl sulfonate, puromycin and DFP. The preparation contained leucyl aminopeptidase and a neutral endopeptidase as contaminating proteases.

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