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NAD(P)H oxidase activity was determined in particulate fractions from human neutrophils by measuring the production of hydrogen peroxide. Activity was measured over a wide range of substrate concentrations from 0.0 to 4.0 mM. The activity with NADPH was consistently greater than with NADH. Activity towards both substrates was higher in a particulate fraction derived from cells which had phagocytized opsonized zymosan than in a corresponding fraction from resting cells. This increased activity was apparently due to a decreased Km of the enzyme, although no evidence of allosteric kinetics was obtained. The activity was markedly reduced in the presence of superoxide dismutase, indicating the involvement of a superoxide-mediated chain reaction. Particular fractions derived from cells of a patient with chronic granulomatous disease exhibited decreased activity towards both substrates and an apparent defect in the activation of the enzyme by phagocytosis.
L R DeChatelet, and
P S Shirley
April 1979,
The Journal of clinical investigation,
L R DeChatelet, and
P S Shirley
May 2003,
International journal of dermatology,
L R DeChatelet, and
P S Shirley
February 1997,
Archives of biochemistry and biophysics,
L R DeChatelet, and
P S Shirley
September 1975,
The New England journal of medicine,
L R DeChatelet, and
P S Shirley
April 1971,
Biochimica et biophysica acta,
L R DeChatelet, and
P S Shirley
September 1985,
Biochemistry international,
L R DeChatelet, and
P S Shirley
January 1994,
Izvestiia Akademii nauk. Seriia biologicheskaia,
L R DeChatelet, and
P S Shirley
January 1982,
Plant physiology,
L R DeChatelet, and
P S Shirley
June 1990,
Inflammation,
L R DeChatelet, and
P S Shirley
April 1997,
Enfermedades infecciosas y microbiologia clinica,
