tailieunhanh - Báo cáo khoa học: A novel metallocarboxypeptidase-like enzyme from the marine annelid Sabellastarte magnifica – a step into the invertebrate world of proteases

After screening 25 marine invertebrates, a novel metallocarboxypeptidase (SmCP) has been identified by activity and MS analytical approaches, and isolated from the marine annelid Sabellastarte magnifica. The enzyme, which is a minor component of the molecularly complex animal body, as shown by 2D gel electrophoresis, has been purified from crude extracts to homogeneity by affinity chromatography on potato carboxypeptidase inhib-itor and by ion exchange chromatography. | A novel metallocarboxypeptidase-like enzyme from the marine annelid Sabellastarte magnifica - a step into the invertebrate world of proteases Maday Alonso-del-Rivero1 Sebastian A. Trejo3 Monica Rodríguez de la Vega3 Yamile Gonzalez1 Silvia Bronsoms3 Francesc Canals2 Julieta Delfin1 Joaquin Diaz1 Francesc X. Aviles3 and María A. Chavez1 1 Centro de Estudio de Proteinas Facultad de Biologia Universidad de la Habana Cuba 2 Institut de Recerca HospitalValld Hebron Barcelona Spain 3 Institut de Biotecnologia i Biomedicina and Departament de Bioquimica i Biologia Molecular Universitat Autonoma de Barcelona Spain Keywords enzyme specificity marine annelid metallocarboxypeptidases metalloproteins Sabellastarte magnifica Correspondence F. X. Aviles Institut de Biotecnologia i Biomedicina IBB and Departament de Bioquimica i Biologia Molecular Universitat Autonoma de Barcelona 08193 Bellaterra Barcelona Spain Fax 34 93 581 2011 Tel 34 93 581 1231 E-mail Received 16 March 2009 revised 16 June 2009 accepted 30 June 2009 doi After screening 25 marine invertebrates a novel metallocarboxypeptidase SmCP has been identified by activity and MS analytical approaches and isolated from the marine annelid Sabellastarte magnifica. The enzyme which is a minor component of the molecularly complex animal body as shown by 2D gel electrophoresis has been purified from crude extracts to homogeneity by affinity chromatography on potato carboxypeptidase inhibitor and by ion exchange chromatography. SmCP is a protease of 33792 Da displaying N-terminal and internal sequence homologies with M14 metallocarboxypeptidase-like enzymes as determined by MS and automated Edman degradation. The enzyme contains one atom of Zn per molecule is activated by Ca2 and is drastically inhibited by the metal chelator 1 10-phenanthroline as well as by excess Zn2 or Cu2 but moderately so by EDTA. SmCP is also strongly inhibited by specific inhibitors of .

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