Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/98823
Type: Artigo de periódico
Title: Trypanosoma Cruzi: Isolation And Characterization Of A Proteinase
Author: Rangel H.A.
Araujo P.M.F.
Repka D.
Costa M.G.
Abstract: Lysates of Trypanosoma cruzi epimastigotes were able to hydrolyze casein (Km = 2.5 mg/ml) as well as bovine and human hemoglobins (Km = 12.2 mg/ml); there was optimum activity was around pH 7.0. The proteinase activity detected with these substrates was enhanced by sodium diaminotetraacetate (EDTA) and reducing agents (SO2- 3, mercaptoethanol, cysteine) and was inhibited by sulfhydryl reagents, thus suggesting an SH-dependent enzyme. Purification (60×) of the proteinase was carried out as follows: (1) precipitation at -20 C, pH 4.5, with 80% acetone, (2) gel filtration on Sephadex G-200, (3) affinity chromatography on Sepharose 4B covalently linked to p-aminophenyl mercuric acetate. Only a single component (with an estimated molecular weight of 60,000) was detected in purified preparations by polyacrylamide gel electrophoresis. However, in addition to the major component identified as a proteinase, crossed immunoelectrophoresis experiments indicated the presence of at least three other antigens that apparently were devoid of proteinase activity. Optimum pH activity of the purified preparations was around pH 6.0 for casein and pH 3.0 for hemoglobins, but these activities probably are due to the one enzyme since they were altered identically by the same agents. © 1981.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/0014-4894(81)90075-8
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0019833366&partnerID=40&md5=7dbf778471d689b52578d29872a86744
Date Issue: 1981
Appears in Collections:Unicamp - Artigos e Outros Documentos

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