1999
DOI: 10.1080/15216549900201483
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Purification and characterization of a novel dipeptidyl peptidase from Dictyostelium discoideum

Abstract: SUMMARY:A dipeptidyl peptidase (DPP) was purified to homogeneity using lys-ala-J~-naphthylamide, the standard substrate for DPP I1. The enzyme is a monomer with a Mr of 70kDa, pl 5.2, and Km 5.0t1M. Its terminal amino acid sequence was XXLLYA|QKRLF and was not identical to that of any known protein. Although initially considered to be a DPP II, the enzyme differed in some properties from classical DPP IIs. It had a pH optimum of 7.9, was not active on X-pro-naphthylamides, the usual substrates of mammalian DPP… Show more

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