کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1941314 1050808 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation
چکیده انگلیسی

Halysase, a hemorrhagic metalloprotease, has an apparent molecular weight of 66 kDa and belongs to the class P-III snake venom metalloprotease. Class P-III snake venom metalloproteases have multifunctional domains including a protease domain and a disintegrin-like domain. Halysase was able to preferentially hydrolyze the α-chain of fibrinogen. Proteolytic activity of the enzyme was completely inhibited by metal chelating agents but not by other typical protease inhibitors. The enzyme principally cleaves X-Leu, X-Tyr, X-Phe, and X-Ala peptide bonds of the oxidized insulin B-chain. Halysase strongly suppresses collagen-induced human platelet aggregation in a dose-dependent manner. Apohalysase that is devoid of its metalloprotease activity was also able to inhibit the platelet aggregation to a certain extent. Experimental evidence clearly indicates that each of the two distinct domains of halysase, the metalloprotease and the disintegrin-like domains, plays its characteristic role to inhibit human platelet aggregation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 339, Issue 3, 20 January 2006, Pages 964–970
نویسندگان
, , , , ,