Abstract
The suitability of octyl-β- d-glucoside as a solubilizing agent for human platelet monoamine oxidase from the outer mitochondrial membrane was investigated and compared to Triton X-100. The properties measured were the effect of the detergents on storage, stability, activity measurements, and solubility of monoamine oxidase, which was measured by pargyline titration. Comparisons on the types of proteins solubilized were also determined by SDS-polyacrylamide gel electrophoresis and isoelectric focusing. Our results demonstrated that octyl-β- d-glucoside was equivalent to purified Triton X-100 and is probably the better detergent for enzyme characterization because of its well-defined chemical composition and its ease of removal by dialysis.
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