Equilibrium binding of myristoyllysophosphatidylcholine to bovine myelin basic protein: An example of ligand-mediated acceptor association

Gow A., Winzor D.J. and Smith R. (1987) Equilibrium binding of myristoyllysophosphatidylcholine to bovine myelin basic protein: An example of ligand-mediated acceptor association. Biochemistry, 26 4: 982-987.

Author Gow A.
Winzor D.J.
Smith R.
Title Equilibrium binding of myristoyllysophosphatidylcholine to bovine myelin basic protein: An example of ligand-mediated acceptor association
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
Publication date 1987
Sub-type Article (original research)
Volume 26
Issue 4
Start page 982
End page 987
Total pages 6
Subject 1303 Specialist Studies in Education
Abstract The interaction of myristoyllysophosphatidylcholine with bovine myelin basic protein at pH 7.4 and 4.5, I = 0.48, has been investigated by a recycling partition equilibrium technique with Bio-Gel P-2 as the gel phase. Important points to emerge from this direct binding study are (i) that it is a monomeric (not micellar) amphiphile that binds to myelin basic protein, (ii) that the amphiphile binds preferentially to the monomeric form of myelin basic protein, (iii) that this binding to monomer is highly cooperative, (iv) that the similarity of binding behavior in the two environments tested is consistent with the dominance of a hydrophobic contribution to the protein-amphiphile interaction, and (v) that the self-association of myelin basic protein in the presence of phospholipid [Smith, R. (1982) Biochemistry 21, 2697-2701] must reflect the aggregation of a protein-amphiphile complex(es) coupled with concomitant release of some lipid. These findings are then related to earlier nuclear magnetic resonance and circular dichroism studies in which the results were interpreted on the basis that myelin basic protein bound preferentially to micellar phospholipid.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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