کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2021769 | 1069263 | 2007 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Isolation, purification and characterization of a DPP-III homologue from goat brain
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 52, Issue 2, April 2007, Pages 297–305
Journal: Protein Expression and Purification - Volume 52, Issue 2, April 2007, Pages 297–305
نویسندگان
Suman Dhanda, Hari Singh, Jasbir Singh, Tej P. Singh,