Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1
AUTOR(ES)
Yang, Yunn-Bor
RESUMO
A d-aminoacylase from Alcaligenes faecalis DA1 has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N-acetyl-dl-methionine as the reaction substrate. The apparent molecular weight and isoelectric point of this enzyme were determined to be 55,000 and 5.4, respectively.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=182879Documentos Relacionados
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