Purification of bovine P2 myelin protein with bound lipids.
The P2 protein is a neuritogenic, small basic protein present in PNS myelin. It belongs to the family of the cytoplasmic lipid-binding proteins and can be incorporated in lipidic bilayers. P2 has been purified and crystallized only in the lipid-free form. Here we show that the P2 protein can be purified with bound lipids by applying to PNS myelin the same procedure that as used to purify lipid-bound myelin basic protein from CNS myelin. SDS-PAGE showed a single band of 16.5 kDa, and TLC showed the presence of most of the myelin lipids associated with the protein. Lipid-bound P2 revealed different circular dichroism spectra from the corresponding lipid-free form, indicating that lipids influence P2 conformation.
Dipartimento di Biologia DBAF, University of Basilicata, Potenza, Italy.
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Riccio
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Zito
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Fasano
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Liuzzi
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Lolli
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Polverini
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Cavatorta
D000818:Animals; D002417:Cattle; D002793:Cholic Acids; D002855:Chromatography, Thin Layer; D002942:Circular Dichroism; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D008055:Lipids / Q000737:chemistry / Q000302:isolation & purification*; D018996:Myelin P2 Protein / Q000737:chemistry / Q000302:isolation & purification*
D002793:Cholic Acids; D003902:Detergents; D008055:Lipids; D018996:Myelin P2 Protein; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate