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A procedure is described for the purification of cytochrome c peroxidase from Pseudomonas aeruginosa involving extraction by sonication, followed by acid precipitation and chromatography on only two types of gel. The final preparation had a purity ratio A407/A280 of 4.2, and was found to be essentially pure by isoelectric focusing. The enzyme was shown to be unstable during degassing under vacuum except in the presence of detergent. The kinetics of CO binding to dithionite-reduced peroxidase were studied with stopped-flow and flash-photolysis techniques, and the results obtained between pH 5 and 7 suggest the existence of two forms of dithionite-reduced enzyme in slow equilibrium.
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
January 1970,
Acta chemica Scandinavica,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
January 1972,
Acta chemica Scandinavica,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
June 1979,
Biochimica et biophysica acta,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
November 1963,
The Biochemical journal,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
May 1992,
Biochimica et biophysica acta,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
May 1982,
The Biochemical journal,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
August 1990,
Biochemistry,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
January 1970,
Acta chemica Scandinavica,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
August 1969,
Proceedings of the National Academy of Sciences of the United States of America,
N Foote, and
A C Thompson, and
D Barber, and
C Greenwood
September 1970,
The Journal of biological chemistry,
