Abstract
A dipeptidyl peptidase (DPP) from goat brain has been purified. The purified enzyme showed a single band on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS–PAGE). It is a monomer with molecular weight of 69 kDa with a p I of 4.5. The K m was estimated to be 39 μM for Arg-Arg-4-methoxy-β-naphthylamide (Arg-Arg-4mβNA). This enzyme is strongly inhibited by commonly used metallochelators and sulfhydryl reagents. Among various β-naphthylamides examined, Arg-Arg-4mβNA was the most rapidly hydrolyzed substrate. Although, initially it was thought to be the DPP-III but on the basis of its molecular weight and inhibition studies, it was concluded that this enzyme is a functional homologue of DPP-III.
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