Cytosolic Components to Activate Neutrophilic NADPH Oxidase in a Cell-Free System

• Published in: Journal of biochemistry (Tokyo) Vol. 108; no. 5; pp. 792 - 797
• Main Authors: Nisimoto, Yukio, Otsuka-Murakami, Hidetsugu
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.11.1990
• Subjects: Analytical, structural and metabolic biochemistry; Antibodies - immunology; arachidonic acid; Biological and medical sciences; Cell-Free System; Cytosol - enzymology; Detergents - pharmacology; Enzyme Activation - drug effects; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Glucosides - pharmacology; Humans; Immunoglobulin G - immunology; Kinetics; magnesium; Molecular Weight; NADH, NADPH Oxidoreductases - immunology; NADH, NADPH Oxidoreductases - metabolism; NADPH oxidase; NADPH Oxidases; NADPH-Ferrihemoprotein Reductase - immunology; Neutrophils - drug effects; Neutrophils - enzymology; Neutrophils - immunology; Nitroblue Tetrazolium - pharmacology; Oxidoreductases; Superoxides - metabolism; NADPH; Purification; Enzymatic activity; Antibody; Gel electrophoresis; Enzyme; HPLC chromatography; Activation; Cytosol; Cell free system

A soluble protein containing very weak NADPH-dependent nitroblue tetrazolium re-ductase activity was partially purified from the cytosol of dormant human neutrophils by DEAE-5PW ion exchange chromatography. This preparation of cytosolic reductase exhibited three nitroblue tetrazolium-reducing bands...