Isolation and purification of myelin basic protein from human brain

Chen, J.; Lai, L.

Hua Xi Yi Ke Da Xue Xue Bao 21(4): 354-356

1990


ISSN/ISBN: 0257-7712
PMID: 1709911
Document Number: 352258
A simplified procedure for isolation and purification of myelin basic protein (MBP) from human brain is described. Purified myelin from white matter was isolated at first, then delipidated with heated organic solvents. The pellet was washed with triethanolamine buffer and extracted with 0.01 mol/L HCl. Finally the protein in the acidic supernatant was purified with Sephadex G-150 column. By using three different PAGE and immunoelectrophoresis, the purified MBP was identified as a homogeneous component with an apparent molecular weight of 18.5 kd and pI 10.6. This procedure has the advantage of simplicity, rapidity, high yield and purity.

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