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Interaction of cations with lipid-free myelin basic protein. A spectroscopy study
P Cavatorta1, S Giovanelli, A Bobba
1Dipartimento di Fisica, Università di Parma.
Acta Neurologica
|April 1, 1991
Abstract:
The interaction of some divalent cations with myelin basic protein (MBP) in buffer and in model membranes was studied by using the static fluorescence of the intrinsic tryptophan residue of the protein. Results were indicative of Zn++ ability to bind to MBP. The observed binding could facilitate the interaction of MBP with lipids and have a role in stabilizing the myelin sheath.