Cytochemical demonstration of negative surface charges in central myelin.
Homogenates of central myelin were treated with ferritin derivatives having different isoelectric points. It was found that considerable amounts of cationic ferritin (pI 8.5-9.5) had access to the extracellular space, but that anionic ferritin (pI 4.0) and native ferritin (pI 4.5) did not. The electrostatic nature of the binding of cationic ferritin was demonstrated by treating the homogenates with poly-L-lysine and 1 M NaCl:both reagents led to a complete displacement of the bound cationic ferritin. Neither extensive trypsination nor neuraminidase treatment showed a significant effect on the intralamellar distribution of the bound cationic ferritin molecules. This suggests that the net negative charge on the extracellular myelin face stems primarily from acidic lipid groups in the membrane.
D000818:Animals; D001921:Brain / Q000166:cytology*; D005293:Ferritins / Q000378:metabolism*; D005614:Freeze Fracturing; D033862:Iron-Binding Proteins; D008563:Membrane Lipids / Q000378:metabolism; D008564:Membrane Potentials; D009186:Myelin Sheath / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism; D009435:Synaptic Transmission
D033862:Iron-Binding Proteins; D008563:Membrane Lipids; D011956:Receptors, Cell Surface; C027293:ferritin receptor; C010297:polycationic ferritin; D005293:Ferritins