Open AccessPurification and subunit determination of the nickel‐dependent Staphylococcus xylosus urease
Author(s) -
Christians Stefan,
Jose Joachim,
Schäfer Udo,
Kaltwasser Heinrich
Publication year - 1991
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.1574-6968.1991.tb04674.x
Subject(s) - urease , staphylococcus xylosus , nickel , chemistry , protein subunit , atomic absorption spectroscopy , molecular mass , enzyme , mass spectrometry , chromatography , bacteria , biochemistry , staphylococcus aureus , nuclear chemistry , staphylococcus , biology , organic chemistry , gene , physics , quantum mechanics , genetics
The Staphylococcus xylosus C2a urease was purified 655‐fold to a maximum specific activity of 1 573 U/mg and contained three non‐identical subunits (64, 17.8 and 16.3 kDa). The purified urease had a total molecular mass of 300 kDa and contained 3.91 ± 0.1 g atoms nickel per molecule as determined by atomic absorption spectrometry. The maximum urease activity occurred at pH 7.2 and 65°C, with a p I between 4 and 5.