Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021769 | Protein Expression and Purification | 2007 | 9 Pages |
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 pI of 4.5. The Km 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.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Suman Dhanda, Hari Singh, Jasbir Singh, Tej P. Singh,