Isolation, purification and characterization of a DPP-III homologue from goat brain

Dhanda, Suman ; Singh, Hari ; Singh, Jasbir ; Singh, Tej P. (2007) Isolation, purification and characterization of a DPP-III homologue from goat brain Protein Expression and Purification, 52 (2). pp. 297-305. ISSN 1046-5928

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S10465...

Related URL: http://dx.doi.org/10.1016/j.pep.2006.10.004

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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Dipeptidyl Peptidase III Homologue; Metalloenzyme; Goat Brain; Arg-Arg-4-methoxy-β-naphthylamide; DPP
ID Code:49136
Deposited On:19 Jul 2011 04:16
Last Modified:19 Jul 2011 04:16

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