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