Myelin basic protein purification in non denaturing conditions.

ABSTRACT

The utilization of denaturing methods for protein purification causes the irreversible loss of quaternary and tertiary structure together with consistent changes in the secondary structure. These modifications reflect on protein antigenicity. MBP is a myelin protein which is bound to membrane-phospholipids. Its tertiary structure is specific for this kind of interaction which determines its native conformation. MBP was obtained in two forms denatured and non denatured. The latter has been purified using the non-ionic detergent beta-octil-D-glucopyranoside which is able to preserve protein tertiary structure separating it from the bilayer phospholipids. Non denaturated MBP could be useful in antibody and/or lymphocyte activity detection studies in various human pathological processes.