Purification of human blood platelet monoamine oxidase.
Monoamine oxidase B has been purified from human blood platelets 185-fold to a specific activity of 113 nmole/min/mg protein by a combination of Triton X-100 solubilization and ion exchange chromatography. A protein fraction corresponding to 58,000 Da on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was identified as monoamine oxidase by its ability to bind [3H]Pargyline.
D001792:Blood Platelets / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008995:Monoamine Oxidase / Q000097:blood / Q000302:isolation & purification*; D017830:Octoxynol; D011092:Polyethylene Glycols
D011092:Polyethylene Glycols; D017830:Octoxynol; D008995:Monoamine Oxidase