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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

Purifica??o e caracteriza??o de uma ?-N-acetillhexosaminadase extra?da do mam?fero marinho Sotalia fluviatilis

Gomes J?nior, Jos? Edilson 06 December 2006 (has links)
Made available in DSpace on 2014-12-17T14:03:42Z (GMT). No. of bitstreams: 1 JoseEGJ.pdf: 604842 bytes, checksum: a34879bd40606d248f800a49ed111824 (MD5) Previous issue date: 2006-12-06 / This report shows 2232 times purification of a βNAcetylhexosaminidase from hepatic extracts from the sea mammal Sotalia fluviatilis homogenate with final recovery of 8,4%. Sequenced steps were utilized for enzyme purification: ammonium sulfate fractionation, Biogel A 1.5 m, chitin, DEAESepharose and hydroxyapatite chromatographies. The protein molecular mass was estimated in 10 kDa using SDSPAGE and confirmed by MALDITOF. It was found to have an optimal pH of 5.0 and a temperature of 60?C. Using pnitrophenylNAcetylβDglycosaminide apparent Km and Vmax values were of 2.72 mM and 0.572 nmol/mg/min, respectively. The enzyme was inhibited by mercury chloride (HgCl2) and sodium dodecil sulfate (SDS) / Este trabalho mostra a purifica??o de 2232 vezes de uma βNAcetilhexosaminidase obtida a partir dos extratos hep?ticos do mam?fero marinho Sotalia fluviatilis com recupera??o final de 8,4%. Passos seq?enciais foram utilizados para a purifica??o enzim?tica: fracionamento com sulfato de am?nio e as cromatografias de Biogel A 1.5 m, Quitina, DEAESepharose e Hidroxiapatita. A massa molecular prot?ica foi estimada em 10 kDa usando SDSPAGE e confirmada por MALDITOF. Foi encontrado como pH e temperatura ?timos, 5,0 e 60?C, respectivamente. Os valores de Km e Vm?x aparentes foram 2,72 mM e 0,572 nmol/mg/min, sendo utilizado o pnitrofenilNAcetilβDglicosamin?deo como substrato. A enzima foi inibida pelo cloreto de merc?rio (HgCl2) e dodecil sulfato de s?dio (SDS)

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