Divalent metals of myelin and their differential binding by myelin basic protein of bovine central nervous system.
Divalent metal ions are being implicated in the compaction of myelin. Levels of Cd, Co, Cu, Hg, Mn, Pb, Zn, Ca and Mg of isolated myelin of bovine central nervous system (CNS) were measured by flame atomic absorption spectrophotometry. Binding of these metal ions by isolated myelin basic protein (MBP, M(r) 18,500) of bovine CNS was concurrently assessed by centrifugal equilibrium dialysis. Metals were bound in the order of Hg > Cu > Zn > Mg > Cd > Co, exempting Mn, Pb and Ca. The results are indicative of differential metal affinity of MBP which may account for the immobilization or anchoring of MBP in myelin by zinc and other divalent metal cations.
Berlet
H H
HH
Institute of Pathochemistry and General Neurochemistry, University of Heidelberg, Germany.
Bischoff
H
H
Weinhardt
F
F
D000818:Animals; D002413:Cations, Divalent / Q000378:metabolism*; D002417:Cattle; D005615:Freezing; D004676:Myelin Basic Protein / Q000378:metabolism*; D009186:Myelin Sheath / Q000378:metabolism*; D011485:Protein Binding; D013054:Spectrophotometry, Atomic; D013116:Spinal Cord / Q000378:metabolism*; D014461:Ultracentrifugation
D002413:Cations, Divalent; D004676:Myelin Basic Protein