Nadph and Nadh Oxidation by Guinea Pig Polymorphonuclear Leucocytes

Iyer, G. Y. N.; Quastel, J. H.

doi:10.1139/o63-051

Cited by 85 publications

(17 citation statements)

References 9 publications

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“…By maintaining granular integrity, cochicine could keep a granule-associated oxidative enzyrie (10)(11)(12) from its soluble substrate. Recent evidence (28), however, suggests that an oxidase for NADH is predominantly located in the nongranular fraction of the cell.…”

Section: Discussionmentioning

confidence: 99%

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The Dissociation by Colchicine of Phagocytosis from Increased Oxygen Consumption in Human Leukocytes*

Malawista¹,

Bodel²

1967

J. Clin. Invest.

160

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Section: Discussionmentioning

confidence: 99%

“…The NADP would be produced during phagocytosis by activation of a pyridine nucleotide oxidase, acting on NADPH either directly or indirectly. Appropriate enzymes have been identified (10)(11)(12), but the steps are not known by which the process of phagocytosis initiates increased oxidase activity.…”

Section: Introductionmentioning

confidence: 99%

The Dissociation by Colchicine of Phagocytosis from Increased Oxygen Consumption in Human Leukocytes*

Malawista¹,

Bodel²

1967

J. Clin. Invest.

160

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“…An enzyme (more accurately, an enzymatic activity) that has been discussed in these terms by several groups of investigators (16)(17)(18)(19) is a NADPH oxidase located in the particulate fraction of neutrophil homogenates. This oxidase has been studied extensively by Rossi and his collaborators (17,18), who characterized it as a manganese requiring enzyme with a pH optimum of 5.5. It has recently become apparent that the manganese requirement is an artifact (20).…”

Section: Introductionmentioning

confidence: 99%

The particulate superoxide-forming system from human neutrophils. Properties of the system and further evidence supporting its participation in the respiratory burst.

Babior¹,

Curnutte²,

McMurrich³

1976

J. Clin. Invest.

326

105

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A B S T R A C T Studies were performed to characterize the previously reported particulate 02-forming system from human neutrophils. Of eight reducing agents examined, including glutathione, ascorbic acid, and intermediates of the glycolytic and hexose monphosphate shunt pathways, only the pyridine nucleotides could serve as electron donors. At 0.1 mM pyridine nucleotide, 02-production was relatively independent of pH. The Km for NADH was approximately 0.7 mM regardless of pH, while with NADPH the Km varied from 0.02 mM at pH 6.0 to 0.3 mM at pH 7.5. The molar ratio of NADPH oxidized to 02-produced was consistent with the reaction: NADPH + 2 02-NADP' + H+; the product nucleotide was shown enzymatically to be NADP. Oa2 production was not inhibited by CN-, N3-, EDTA, or 1,10-phenanthroline. Particulate 02-production accounted for 35% of the oxygen taken up during the respiratory burst by an equivalent number of intact neutrophils.Greatly diminished Oa-production was seen with particles prepared from cells obtained from three patients with chronic granulomatous disease, with 2.5 mM NADPH as electron donor. With 5.0 mM NADH similar observations were made with particles from two of the patients, but with this nucleotide, 02-production was only slightly reduced in the third case.The evidence available suggests that this particulate 02i-forming system is the one responsible for the respiratory burst in activated neutrophils. The relationship between this system and other 02i-forming system found in human neutrophils is discussed.

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“…Major controversy has arisen over which nucleotide is oxidized, and evidence for both NADH and NADPH has been advanced (14)(15)(16)(17)(18)(19). There is agreement that the controlling factor for HMIPS activity is the availability of NADP+ (20).…”

Section: Introductionmentioning

confidence: 99%