Purification of human placenta diamine oxidase.
Diamine oxidase (histaminase) is produced at very high levels by the decidual cells of the placenta. The presence of diamine oxidase has been demonstrated in human neutrophils. Purification of human placenta diamine oxidase was performed by four subfractionation steps and led to the isolation of one polypeptide whose molecular weight was 84,000, as assessed by SDS PAGE. Using polyclonal antibodies raised against the purified enzyme, we have demonstrated that the neutrophil diamine oxidase is immunochemically identical to the placental diamine oxidase. Development of immunological methods will be useful for detection and quantitation of diamine oxidase in neutrophils during the inflammation process.
Morel
F
F
Laboratoire d'Enzymologie, Centre Hospitalier Universitaire, Grenoble, France.
Surla
A
A
Vignais
P V
PV
D006631:Amine Oxidase (Copper-Containing) / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D015153:Blotting, Western; D002845:Chromatography; D005089:Exocytosis; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D006631:Amine Oxidase (Copper-Containing); D000645:Ammonium Sulfate