کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8332928 | 1540253 | 2014 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of a Kunitz-type protease inhibitor peptide (Rusvikunin) purified from Daboia russelii russelii venom
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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
The snake venom may be considered as a potent source of untapped therapeutic proteins and peptides. The peptide mass fingerprinting and N-terminal sequence alignment of a 6.9 kDa peptide named Rusvikunin from Daboia russelii russelii venom show the presence of putative conserved domains of the KU superfamily. Further, BLAST analysis of two of the de novo peptide sequences of Rusvikunin demonstrates significant sequence homology with serine proteases reported in the NCBI database. Rusvikunin possesses conserved cysteine residues and Arg15 at the P1 position. It inhibits amidolytic activity of trypsin (IC50 = 50 nmol/l), plasmin (IC50 = 1.1 μmol/l), and fibrinogen clotting as well as plasma clotting activity of thrombin (IC50 = 1.3 μmol/l); however, it does not inhibit the amidolytic activity of chymotrypsin, thrombin, factor Xa, and tissue plasminogen activator. Rusvikunin is a glycoprotein, demonstrates dose-dependent BAEE-esterase activity. It does not show lethality in mice or in vitro cytotoxicity against mammalian cells but shows in vivo anticoagulant activity 6 h after i.p. injection in the mouse model. The commercial polyvalent and monovalent antivenom failed to inhibit the functional properties of Rusvikunin. The possible biomedical applications of Rusvikunin in the treatment and/or prevention of cardiovascular disorders such as thrombosis and trypsin-induced inflammation are suggested.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 67, June 2014, Pages 154-162
Journal: International Journal of Biological Macromolecules - Volume 67, June 2014, Pages 154-162
نویسندگان
Ashis K. Mukherjee, Stephen P. Mackessy, Sumita Dutta,