Protein Expression and Purification

Texto completo. Acesso restrito. p. 355–366 Submitted by Santiago Fabio (fabio.ssantiago@hotmail.com) on 2013-09-09T18:03:41Z No. of bitstreams: 1 11111111.pdf: 374080 bytes, checksum: 95febf9cb2121d9cf26a5318582ba2d8 (MD5) Approved for entry into archive by Rodrigo Meirelles (rodrigomei@ufba.br) on 2013-11-16T13:15:44Z (GMT) No. of bitstreams: 1 11111111.pdf: 374080 bytes, checksum: 95febf9cb2121d9cf26a5318582ba2d8 (MD5) Made available in DSpace on 2013-11-16T13:15:44Z (GMT). No. of bitstreams: 1 11111111.pdf: 374080 bytes, checksum: 95febf9cb2121d9cf26a5318582ba2d8 (MD5) Previous issue date: 1996 The azurophil granules of human PMN contain four antibiotic proteins, the serprocidins, which have extensive homology to one another and to serine proteases. Azurocidin, a member of this family, is a 29-kDa glycoprotein with broad spectrum antimicrobial activity and chemotactic activity toward monocytes. Insect cells transfected with a baculovirus vector carrying azurocidin cDNA produced a recombinant azurocidin protein. We purified the recombinant azurocidin protein from the culture medium of the infected cells and showed that it retained the antimicrobial activity of the native neutrophil-derived molecule. In addition, we present evidence that a 49-amino-acid region of the recombinant azurocidin protein is required for its secretion from insect cells. Salvador