Purificação e caracterização da arilsulfatase A de parotida bovina
AUTOR(ES)
Ana Claudia de Melo Stevanato Nakamune
DATA DE PUBLICAÇÃO
2002
RESUMO
Arylsulfatase A from bovine parotid was purified 6,614-fold to homogeneity, by procedures involving ammonium sulfate fractionation, acid treatment, acetone preciptation, DEAE-Sephadex ion-exchange chromatography and Sephacryl S-200 gel filtration. The enzyme recovery was 35.1 % and specific activity 79.4 units per mg protein. The following homogeneity criteria were used: PAGE, SDS-PAGE and gel filtration on Sephacryl-S200. The relative molecular mass of 135.0 (dimer) and 60.5 kDa (monomer) were determined by gel filtration chromatography and SDSPAGE, respectively. Kinectic studies showed an optimum temperature of 40° C, and a broad optimum pH between 4.5-5.5. The I glandulas parotidas glandulas salivares
ASSUNTO(S)
ACESSO AO ARTIGO
http://libdigi.unicamp.br/document/?code=vtls000256984
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