Identification of S‐100 proteins and S‐ 100‐binding proteins in a detergent‐resistant EDTA/KCl‐extractable fraction from bovine brain membranes

FEBS Letters

Ceccarelli, Paolo¹  Aisa, Maria Cristina¹  Giambanco, lleana¹  Donato, Rosario¹ 

[1] Section of Anatomy, Department of Experimental Medicine and Biological Sciences, Cas. Post. 81, 06100 Perugia Succ. 3, Italy

关键词: Protein;    S-100;    Membrane protein;    Cytoskeleton;    Ca2+;   

DOI  :  10.1016/0014-5793(89)81234-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺ 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 Ca²⁺ 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 Ca²⁺-regulated. Several S-100-binding proteins are identified in the detergent-resistant residue of brain membranes by an overlay procedure.

【 授权许可】

Unknown