-transparent.png){kind=logo}
Human eosinophil peroxidase is a cationic protein with a higher content of arginine, the enzyme being poorly soluble in water. The purified enzyme is able to carry out the peroxidative chlorination of monochlorodimedon. Like myeloperoxidase the position of the pH optimum of this reaction depends on the ration of the concentrations of chloride and H2O2. Compared to myeloperoxidase the pH optimum is shifted by 0.8 pH unit to more acid pH values. The physiological consequences of the properties of the eosinophil peroxidase are discussed.
Related Publications
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
January 1984,
Acta haematologica,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
May 1974,
Blood,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
November 1994,
The Journal of biological chemistry,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
September 1986,
Journal of immunology (Baltimore, Md. : 1950),
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
September 2002,
The Journal of allergy and clinical immunology,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
July 1988,
Immunology,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
April 1991,
Cellular immunology,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
June 1977,
Histochemistry,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
February 1978,
Biochemical medicine,
R Wever, and
M N Hamers, and
C J de Graaf, and
R S Weening, and
D Roos
August 1985,
The Biochemical journal,
