Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study.

Biochemistry
M B SankaramD Marsh

Abstract

The myelin basic protein (MBP) from bovine spinal cord was cleaved at the single tryptophan residue to produce an N-terminal fragment (F1) of molecular weight 12.6K and a C-terminal fragment (F2) of molecular weight 5.8K. The interactions of the two fragments with bilayers of the acidic lipid dimyristoylphosphatidylglycerol (DMPG) were compared with those of the intact protein, by using both chemical binding assays and spin-label electron spin resonance spectroscopy. The saturation binding stoichiometries of the two fragments were found to sum to that of the MBP, having values of 11, 24, and 36 mol of DMPG/mol of protein for F2, F1, and the MBP, respectively. The strength of binding was found to increase in the order F2 less than F1 less than MBP, which follows that of the net charges on the different fragments. The ionic strength dependence of the protein binding indicated that the interaction is primarily of electrostatic origin. The efficiency of displacement of the proteins by salt was in the order F2 greater than F1 greater than MBP, which correlates with both the strength of binding and the net charge on the different protein fragments. Nitroxide derivatives of phosphatidylglycerol (PG) labeled on the sn-2 chain were used...Continue Reading

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Citations

Jan 1, 1991·The International Journal of Biochemistry·T Cserháti, M Szögyi
Jun 26, 1998·Progress in Lipid Research·I Ishizuka
Apr 16, 2003·Micron : the International Research and Review Journal for Microscopy·Christopher M D HillGeorge Harauz
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Aug 2, 2008·Methods : a Companion to Methods in Enzymology·Derek Marsh
Feb 26, 2008·Biochimica Et Biophysica Acta·Derek Marsh
Mar 19, 1991·Biochemistry·P MeersD Papahadjopoulos
Nov 1, 1992·Journal of Neurochemistry·R Smith

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