Purification, characterization and ion binding properties of human brain S100b protein.

  title={Purification, characterization and ion binding properties of human brain S100b protein.},
  author={Jacques Baudier and Nicole Glasser and Kenneth G. Haglid and Dominique G{\'e}rard},
  journal={Biochimica et biophysica acta},
  volume={790 2},
S100 Proteins: Structure and Calcium Binding Properties
The highly acidic water-soluble protein, S100 (Moore 1965) is a group of closely related proteins which, when purified, appear as non-covalent dimers with subunit composition αα (S100αα), αβ (S1000a)
S-100 proteins.
Specificity and Zn2+ Enhancement of the S100B Binding Epitope TRTK-12*
Interactions of TRTK-12 with S100B have been shown to be calcium-sensitive and enhanced by zinc binding, resulting in an approximate 5-fold decrease in the TRTk-12/S100B dissociation constant.
Binding study of metal ions to S100 protein: 43Ca, 25Mg, 67Zn and 39K n.m.r.
Mechanisms of Action of the S100 Family of Calcium Modulated Proteins
Eukaryotic cells require calcium ions for optimal growth and functioning. The intracellular actions of calcium as a biological second messenger appear to be a result of its interaction with a set of
The role of zinc in the S100 proteins: insights from the X-ray structures
A broader knowledge of the role of zinc in the functioning of the S100 proteins will add significantly to the understanding how they propagate their signals.
Brain- and heart-type fatty acid-binding proteins in the brain: tissue distribution and clinical utility.
Investigation of the tissue distribution of brain- and heart-type fatty acid-binding proteins in segments of the human brain and the potential of either protein to serve as plasma marker for diagnosis of brain injury indicates that B-FABP and H-FabP are more sensitive markers for minor brain injury than the currently used markers S100B and NSE.
The Zn2+ and Ca2+‐binding S100B and S100A1 proteins: beyond the myths
A new consensus S100B binding motif present in intracellular and extracellular vertebrate‐specific proteins is described and a new model for stable interactions of S 100B dimers with full‐length target proteins is proposed.
Structure/function studies of S100A8/A9
This review focuses on the structure and post-translational modifications of mS100A8/A9 and their effects on function, particularly chemotaxis.


Reinvestigation of extremely acidic proteins in bovine brain.
Peripheral distribution of nervous system-specific S-100 protein in rat.
The S-100 protein levels in several tissues were significantly higher in female rats than in males at ages of 5 to 6 weeks, and in adipose tissue and in trachea, which involves cartilage.
The Amino-Acid Sequence of the α Subunit in Bovine Brain S-100a Protein
The sequence of the α subunit in the S-100a protein shows extensive homology with that of the β-subunit and shares an apparent calcium binding site in the C-terminal half of the molecule, suggesting a close evolutionary relationship between these subunits.
Bovine Brain S100 Proteins: Separation and Characterization of a New S100 Protein Species
Characterization by urea/sodium dodecyl sulfate/polyacrylamide gel electrophoresis, UV absorption spectra, and fluorescence parameters provided evidence of anew tryptophan‐containing S100 protein called S100a′, which exhibits the properties of a Ca2+ binding protein.
Modulation of brain protein phosphorylation by the S-100 protein.