Lipid-bound, native-like, myelin basic protein

Abstract

Batch purification of the myelin basic protein (MBP) in the lipid-bound form was obtained from bovine brain white matter by using the slightly polydisperse nonionic detergent, n-octyl-pentaoxyethylene (octyl-POE) and hydroxyapatite. This large-scale procedure can also be carried out in laboratories without chromatographic equipment, and is applicable to small amounts of myelin. More interestingly, removal and inhibition of the proteolytic activity associated with myelin allowed us to obtain more stable and intact forms of the protein when compared with MBP isolated in the lipid-bound form by our previous method. Since it retains binding to all myelin lipids, this purified MBP may be considered as being in a native-like form. In this article, we suggest why this more intact form of MBP could be used to advantage as an alternative to lipid-free, water-soluble MBP in the study, detection, and treatment of myelin damage in pathology.