Purification and partial characterization of mammalian Cu-dependent amine oxidases.
Bovine serum amine oxidase, porcine kidney diamine oxidase and human placental and pregnancy serum diamine oxidases have been purified by affinity chromatography and ion exchange chromatography. The purified enzymes were subjected to peptide mapping studies with trypsin, S. aureus V8 protease and pepsin. These studies revealed similarities between the enzymes and partial sequences from the bovine serum amine oxidase were obtained. The sequences obtained showed no homology to known sequences. Immunological studies using monoclonal antibodies to the purified enzymes revealed cross reactivity between the four enzymes. These results support the view that the Cu-dependent amine oxidases constitute a closely related group (E.C. 1.4.3.6).
Houen
G
G
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Jørgensen
J
J
Leonardsen
L
L
Larsson
L I
LI
D006631:Amine Oxidase (Copper-Containing) / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D007120:Immunochemistry; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D013552:Swine
D006631:Amine Oxidase (Copper-Containing)