Purification and some properties of diamine oxidase from pig kidney and human placenta.
1. A homogeneous preparation of pig kidney diamine oxidase was obtained by polyacrylamide gel electrophoresis and immunodiffusion. Its molecular weight was estimated as 170,000 by Sephadex G-200 column chromatography and as 220,000 by SDS-polyacrylamide gelelectrophoresis. After mercaptoethanol cleavage of disulfide bonding, the molecular weight of the subunit was 130,000. 2. Little contamination was observed in the preparation of human placenta by SDS-polyacrylamide gel electrophoresis and immunoelectrophoresis and the molecular weight was calculated as 30008000 and 280,000 by the extrapolation from the calibration curve of Sephadex G-200 column chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The subunit was 170,000. 3. By immunodiffusion, immunoelectrophoresis and inhibition test of the enzyme activity using a heterologous antiserum, a good cross-reactivity was observed between the anti-human diamine oxidase serum and pig diamine oxidase. 4. The activities of the two enzymes were not almost inhibited by homologous and heterologous antisera.
D006631:Amine Oxidase (Copper-Containing) / Q000037:antagonists & inhibitors / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D008958:Models, Molecular; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine
D006631:Amine Oxidase (Copper-Containing)