Abstract
Publisher Summary This chapter focuses on nicotinamide adenine dinucleotide (NADH) oxidase enzyme system from guinea pig polymorphonuclear leukocytes (PMN). This oxidase from guinea pig PMN catalyzes a cyanide-insensitive production of H 2 O 2 from NADH. Superoxide (O 2 – ) is produced as an intermediate during this reaction. For every 1.0 nmol of NADH oxidized, only 0.3 nmol of O 2 – is produced. In addition, this stoichiometry is consistent with two modes of electron release from the enzyme—namely, (1) a divalent pathway that results in the direct transfer of two electrons to O 2 to produce H 2 O 2 and (2) a univalent pathway that involves the transfer of single electrons to O 2 to produce O 2 – . NADH-oxidase is thought to function as a peripheral membrane protein in association with the cytoplasmic surface of the phagosomal membrane. Guinea pig neutrophils contain high levels of an aldehyde oxidase that also produces O 2 – and H 2 O 2 . The oxidation of NADH is followed spectrophotomctrically at 340 nm. This reaction measures all NADH-oxidizing activities present in a given sample.
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