Identification and Characterization of Sulfhydryl-Containing Proteolytic Fragments Involved in the Ca2+-Induced Conformational Change of Beef Brain S-100
Article first published online: 5 OCT 2006
Journal of Neurochemistry
Volume 39, Issue 3, pages 601–612, September 1982
How to Cite
Nika, H., Haglid, K. G., Wrońki, A. and Hansson, H.-A. (1982), Identification and Characterization of Sulfhydryl-Containing Proteolytic Fragments Involved in the Ca2+-Induced Conformational Change of Beef Brain S-100. Journal of Neurochemistry, 39: 601–612. doi: 10.1111/j.1471-4159.1982.tb07936.x
- Issue published online: 5 OCT 2006
- Article first published online: 5 OCT 2006
- Received August 21, 1981; accepted February 8, 1982.
- S-100 protein;
- Ca2+- dependent conformational change;
- Proteolytic fragments
Abstract: The Ca2+-dependent conformational alteration of the brain-specific S-100 protein was studied by reacting the protein with N-ethyl[2,3-14C]maleimide in the absence and presence of Ca2+ and under denaturing conditions. Peptic hydrolysates of the 14C-labeled protein were analyzed and fractionated by high-performance liquid chromatography. Labeled peptide fractions were characterized by high-voltage electrophoresis and TLC. A clear distinction could be made between two classes of sulfhydryl-containing fragments: (a) neutral, hydrophobic, and (b) acidic. Ca2+ markedly favored 14C incorporation into the former components, whereas the latter were readily available only under denaturing conditions.