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Literature summary for 1.6.2.4 extracted from

  • Laporte, F.; Doussiere, J.; Vignais, P.V.
    Properties of the NADPH dehydrogenase component of the oxidase complex from rabbit peritoneal neutrophils: reconstitution of an oxidase activity with the dehydrogenase component and a membrane extract (1990), Biochem. Biophys. Res. Commun., 167, 790-797.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Mersalyl
-
Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
77000
-
x * 77000, SDS-PAGE Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
sequential chromatography on DE 52 cellulose and 2',5'-ADP Sepharose Oryctolagus cuniculus

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of O2- generating system Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
neutrophil peritoneal Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH additional electron acceptor: benzylviologen Oryctolagus cuniculus 2 ferrocytochrome c + NADP+ + H+
-
?

Subunits

Subunits Comment Organism
? x * 77000, SDS-PAGE Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Oryctolagus cuniculus
FMN
-
Oryctolagus cuniculus
NADPH higher activity towards NADPH than towards NADH Oryctolagus cuniculus