Veterinary Parasitology

Autor: Alves, J. L., Lima, F. W. Mendonça, Alves, C. R.
Jazyk: angličtina
Rok vydání: 2004
Předmět:
Zdroj: Repositório Institucional da UFBA
Universidade Federal da Bahia (UFBA)
instacron:UFBA
ISSN: 0304-4017
DOI: 10.1016/j.vetpar.2003.11.005
Popis: Texto completo: acesso restrito. p. 137-145 Submitted by JURANDI DE SOUZA SILVA (jssufba@hotmail.com) on 2013-01-31T18:23:43Z No. of bitstreams: 1 1-s2.0-S0304401703004631-main.pdf: 123031 bytes, checksum: c95076819277476df528e7869138f780 (MD5) Approved for entry into archive by Alda Lima da Silva(sivalda@ufba.br) on 2013-01-31T20:00:13Z (GMT) No. of bitstreams: 1 1-s2.0-S0304401703004631-main.pdf: 123031 bytes, checksum: c95076819277476df528e7869138f780 (MD5) Made available in DSpace on 2013-01-31T20:00:13Z (GMT). No. of bitstreams: 1 1-s2.0-S0304401703004631-main.pdf: 123031 bytes, checksum: c95076819277476df528e7869138f780 (MD5) Previous issue date: 2004 In this work, we have assessed the possibility of isolating metalloproteinase fractions from infective Leishmania chagasi promastigotes. Our strategy was the association of the Triton X-114 method with iminodiacetic chromatography enriched with Zn2+. Thus, by using acid conditions, it was possible to isolate two fractions containing two polypeptides, 59 and 63 kDa. The enzymatic activity assay indicated that the two fractions and the two polypeptides had proteinase activities. In addition, it was proposed that those proteinase activities were affected by the presence of 1,10-phenanthroline, a metalloproteinase inhibitor. With this gentle chromatography strategy proposed it is possible to obtain metalloproteinases from L. chagasi in folding that preserve the enzyme activity. This is important for further studies on pathological complications observed in visceral leishmaniasis.
Databáze: OpenAIRE
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