THE NATURE OF THE ELECTROPHORETICALLY SEPARABLE FORMS OF MONOAMINE OXIDASE

作者: MILES D. HOUSLAY , KEITH F. TIPTON

DOI: 10.1016/B978-0-08-017922-3.50025-3

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摘要: Publisher Summary This chapter elaborates a study analyzing the nature of electrophoretically separable forms monoamine oxidase. Chaotropic agents have been shown to disrupt protein-lipid complexes by weakening hydrophobic bonds. In this study, chaotropic agent, sodium perchlorate, was used investigate Triton X-100 solubilized mitochondrial oxidase from rat liver and human brain. Polyacrylamide gel electrophoresis preparations gave rise number bands activity, although with enzyme band activity which remained at origin found be an artifact loading procedure. After treatment only single could detected. case enzyme, had phospholipid content similar that most mobile cathodically (least containing) untreated enzyme. Gel filtration perchlorate-treated on Sepharose 4B indicated no appreciable change in molecular weight occurred, however opalescent fraction separated rich lipids, whilst little such material

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