| Literature DB >> 17320169 |
Rodrigo G Stábeli1, Carolina D Sant'Ana, Patrícia H Ribeiro, Tássia R Costa, Fábio K Ticli, Matheus G Pires, Auro Nomizo, Sérgio Albuquerque, Natael R Malta-Neto, Mozart Marins, Suely V Sampaio, Andreimar M Soares.
Abstract
An L-amino acid oxidase isolated from Bothrops moojeni snake venom (BmooLAAO-I) was purified to a high degree using sequential CM-Sepharose ion-exchange and phenyl-Sepharose chromatography. When analyzed by mass spectrometry, the purified BmooLAAO-I presented a molecular weight of 64,889 and 130,779 under denaturing and nondenaturing conditions, respectively. BmooLAAO-I is a homodimeric acidic glycoprotein with a pI approximately 4.7, and the N-terminal sequence shows close structural similarity to other snake venom LAAOs. This enzyme was inactivated by freezing or low pH, and secondary structural analysis by circular dichroism revealed 48% alpha-helix, 20% beta-sheet, 12% beta-turn, and 20% random coil structures. BmooLAAO-I exhibited bactericidal, antitumoral, trypanocidal, edematogenic, and platelet-aggregating activities. All of these effects were inhibited by catalase, suggesting that these biological effects are mediated by the production of H(2)O(2). BmooLAAO-I induced typical apoptotic DNA fragmentation in HL-60 cells, which was also inhibited by catalase. These results point to the potential use of BmooLAAO-I as a therapeutic agent for treatment of diseases in which induction of H(2)O(2) production can be beneficial.Entities:
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Year: 2007 PMID： 17320169 DOI： 10.1016/j.ijbiomac.2007.01.006
Source DB: PubMed Journal: Int J Biol Macromol ISSN： 0141-8130 Impact factor: 6.953