title: Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1.
abstract: 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.
authors.affiliation: Institute of Biochemistry, National Yang-Ming Medical College, Taipei 11221, Taiwan, Republic of China.
authors.forename: Y B
authors.initials: YB
authors.lastname: Yang
authors.forename: C S
authors.initials: CS
authors.lastname: Lin
authors.forename: C P
authors.initials: CP
authors.lastname: Tseng
authors.forename: Y J
authors.initials: YJ
authors.lastname: Wang
authors.forename: Y C
authors.initials: YC
authors.lastname: Tsai