Developmental & Comparative Immunology 2001-01-01

NADPH and NADH serve as electron donor for the superoxide-generating enzyme in tilapia (Oreochromis niloticus) neutrophils.

T Shiibashi, T Iida

Index: Dev. Comp. Immunol. 25(5-6) , 461-5, (2001)

Full Text: HTML

Abstract

NADPH oxidase has been identified as the superoxide-generating enzyme in fish neutrophils. To clarify the electron-donating ability of this enzyme, we examine the requirement of NADPH as the electron donor in superoxide generation in tilapia (Oreochromis niloticus) neutrophils using CLA-dependent chemiluminescence (CL). Phorbol ester-induced CL responses were terminated upon the addition of a detergent, Renex-30. The addition of graded amounts of NADPH or NADH restored the CL in a dose-dependent manner. The restoration of CL was completely eliminated by superoxide dismutase, suggesting that the restored CL was due to superoxide generation. NADPH tended to have a greater effect than NADH on the CL responses of tilapia neutrophils.


Related Compounds

Related Articles:

Pitfalls in the use of commercial nonionic detergents for the solubilization of integral membrane proteins: sulfhydryl oxidizing contaminants and their elimination.

1980-05-01

[Anal. Biochem. 104(1) , 112-7, (1980)]

Evaluation of the single radial-immunodiffusion assay for measuring the glycoprotein content of rabies vaccines.

1987-01-01

[J. Biol. Stand. 15(1) , 1-10, (1987)]

Horse kidney neutral alpha-D-glucosidase: purification of the detergent-solubilized enzyme; comparison with the proteinase-solubilized forms.

1985-09-20

[Biochim. Biophys. Acta 831(1) , 59-66, (1985)]

Phospholipid solubilization during detergent extraction of rhodopsin from photoreceptor disk membranes.

1995-12-20

[Arch. Biochem. Biophys. 324 , 331-343, (1995)]

Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity: direct evidence for NADPH as the predominant electron donor to oxygen in phagocytizing human neutrophils.

1981-02-12

[Biochem. Biophys. Res. Commun. 98(3) , 743-51, (1981)]

More Articles...