A Boophilus microplus vitellin-degrading cysteine endopeptidase

dc.creatorSeixas, Adriana
dc.creatorSantos, Patricia Coutinho dos
dc.creatorVelloso, Fernando F.
dc.creatorVaz Junior, Itabajara da Silva
dc.creatorMasuda, Aoi
dc.creatorHorn, Fabiana
dc.creatorTermignoni, Carlos
dc.date2011-01-21T05:59:00Z
dc.date2003
dc.identifier0031-1820
dc.identifierhttp://hdl.handle.net/10183/27453
dc.identifier000353397
dc.descriptionHere we describe the purification and characterization of a vitellin (VT) degrading cysteine endopeptidase (VTDCE) from eggs of the hard tick Boophilus microplus. A homogeneous enzyme preparation was obtained by chromatographic fractionation on ion-exchange and gel filtration columns and an autolysis step. This step consisted of incubation of a semipurified enzyme (after the first ion-exchange chromatography) at pH 4.0 that dissociated the enzyme from VT, to which VTDCE is naturally tightly associated. The enzyme purity was confirmed by capillary and native gel electrophoresis, and SDS–PAGEsuggested the enzyme is a dimer of 17 and 22 kDa.VTDCEwas active upon several synthetic substrates, with a preference for a hydrophobic or a basic residue in P1, and a hydrophobic residue in P2. VTDCE also hydrolysed haemoglobin, albumin, gelatin and vitellin.VTDCEis inactive in the absence ofDTTand was totally inhibited by E-64, indicating it is a cysteine endopeptidase. Our results suggest that VTDCE is a major enzyme involved in yolk processing during B. microplus embryogenesis.
dc.formatapplication/pdf
dc.languageeng
dc.relationParasitology. Cambridge, United Kingdom. Vol. 126, (2003), p. 155-163
dc.rightsOpen Access
dc.subjectTick
dc.subjectBoophilus microplus
dc.subjectCysteine endopeptidase
dc.subjectVitellin
dc.subjectEmbryogenesis
dc.subjectBoophilus microplus : Cystein endopeptidase
dc.subjectBioquímica
dc.titleA Boophilus microplus vitellin-degrading cysteine endopeptidase
dc.typeArtigo de periódico
dc.typeEstrangeiro


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