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|Type:||Artigo de periódico|
|Title:||Purification and Characterization of a New Weak Hemorrhagic Metalloproteinase BmHF-1 from Bothrops marajoensis Snake Venom|
|Abstract:||BmHF-1, from the venom of Bothrops marajoensis, was purified by Sephadex G-75 and HPLC-RP on mu-Bondapak C-18 column chromatography. It presented a molecular mass of 27162.36 Da determined by MALDI-TOF MS. BmHF-1 had a sequence of 238 residues of amino acids. The multiple alignment of its amino acid sequence and those of other snake venom metalloproteinases showed high structural similarity, mainly among P-I class. The enzyme initially cleaves the A alpha-chain of fibrinogen, followed by the B beta-chain, and shows no effects on the gamma-chain. BmHF-1 had, caseinolytic and weakly hemorrhagic activities, which were inhibited by EDTA. In contrast, PMSF did not affect these activities. The caseinolytic activity of BmHF-1 had a pH optimum of 8.0 and was stable in solution up to 40 A degrees C; activity was completely lost at a parts per thousand yen70 A degrees C. The proteolytic activity was also inhibited by sDa (opossum sera) and Da2-1, Da2-II, antihemorrhagic factors isolated from the opossum sera of Didelphis albiventris. BmHF-1 presents weak hemorrhagic activity, with a MHD of 41.14 mu g and it induces dose-dependent edema. We could concluded that, despite its weak hemorrhagic activity, BmHF-1 contributes to local tissue damage by inducing edema, releasing pharmacologically active mediators from protein precursors due to its enzymatic action.|
Snake venom metaloproteases
|Citation:||Protein Journal. Springer, v. 29, n. 6, n. 407, n. 416, 2010.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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