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Identification of S‐100 proteins and S‐ 100‐binding proteins in a detergent‐resistant EDTA/KCl‐extractable fraction from bovine brain membranes
Author(s) -
Donato Rosario,
Giambanco lleana,
Aisa Maria Cristina,
Ceccarelli Paolo
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81234-7
Subject(s) - membrane , chemistry , residue (chemistry) , triton x 100 , membrane protein , lipid bilayer , chromatography , solubilization , fraction (chemistry) , biochemistry , pulmonary surfactant
The Triton X‐100‐resistant residue of brain membranes contains appreciable amounts of S‐100 proteins. This fraction of S‐100 can be solubilized by high concentrations of EDTA plus or minus high concentrations of KCl. Whereas KCl (0.6 M) extracts the detergent‐resistant S‐100, NACl (1 M) does not. Endogenous Ca 2+ is required and is sufficient for S‐100 to remain associated with the detergent‐resistant residue. However, 0.6 M KCl extracts a further fraction of Triton X‐100‐resistant S‐100. In contrast, the Triton X‐100‐extractable fraction of S‐100 resists the action of EDTA. These data suggest that Ca 2+ regulates the extent of association of S‐100 with Triton X‐100‐resistant components in brain membranes, whereas the association of S‐100 with the lipid bilayer of brain membranes and/or with some intrinsic membrane proteins is less Ca 2+ ‐regulated. Several S‐100‐binding proteins are identified in the detergent‐resistant residue of brain membranes by an overlay procedure.