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
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
---|---|
Data(s) |
20/05/2014
20/05/2014
01/06/2004
|
Resumo |
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. |
Formato |
281-284 |
Identificador |
http://dx.doi.org/10.1016/j.bbapap.2004.02.005 Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004. 1570-9639 http://hdl.handle.net/11449/17577 10.1016/j.bbapap.2004.02.005 WOS:000221807800030 |
Idioma(s) |
eng |
Publicador |
Elsevier B.V. |
Relação |
Biochimica et Biophysica Acta: Proteins and Proteomics |
Direitos |
closedAccess |
Palavras-Chave | #crystallization #X-ray crystallography #acidic phospholipase A(2) #Bothrops jararacussu venom #alpha-tocopherol #p-bromophenacyl bromide |
Tipo |
info:eu-repo/semantics/article |