Open AccessPurification and partial characterization of two azoreductases from Shigella dysenteriae Type 1
Author(s) -
Ghosh Dilip K.,
Mandal Amalendu,
Chaudhuri Jayasri
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05519.x
Subject(s) - amaranth , shigella dysenteriae , chemistry , tartrazine , orange (colour) , monomer , biochemistry , chromatography , nuclear chemistry , food science , organic chemistry , escherichia coli , polymer , gene
Two azoreductases (I and II) were purified to homogeneity from extracts of Shigella dysenteriae (type 1). Azoreductase I was a dimer of identical subunits of M r 28 000, whereas azoreductase II was a monomer of 11 000 M r . Both were flavoproteins, each containing 1 mol of FMN per mol enzyme. Both NADH and NADPH functioned as electron donors for the azoreductases. Azoreductase I used Ponceau SX, Tartrazine, Amaranth and Orange II as substrates. Azoreductase II utilized all the dyes except Amaranth.