Please use this identifier to cite or link to this item:
- Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolution
- Universidade Estadual Paulista (UNESP)
- An acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-Angstrom resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred. (C) 2004 Elsevier B.V. All rights reserved.
- Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004.
- Elsevier B.V.
- X-ray crystallography
- acidic phospholipase A(2)
- Bothrops jararacussu venom
- p-bromophenacyl bromide
- Acesso restrito
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.