Zinc‐dependent affinity chromatography of the S100b protein on phenyl—Sepharose
- 8 November 1982
- journal article
- Published by Wiley in FEBS Letters
- Vol. 148 (2) , 231-234
- https://doi.org/10.1016/0014-5793(82)80813-2
Abstract
A rapid high resolution method of purification of the Trp-containing S100 proteins (S100a, S100a′) and of the S100b protein has been developed. The principle of this method is based on the fact that S100b protein becomes highly hydrophobic upon Zn2+ binding, whereas S100a and S100a′ are not affected. On an affinity chromatography of phenyl—Sepharose column, S100b is selectively bound in presence of zinc, whereas the Trp-containing S100 patients are quickly eluted. The S100b protein is further eluted with a buffer containing EDTA.Keywords
This publication has 8 references indexed in Scilit:
- Physicochemical and optical studies on the calcium- and potassium-induced conformational changes in bovine brain S-100b proteinBiochemistry, 1982
- LOCALIZATION OF S100 PROTEIN IN THE RAT CEREBELLUM: AN IMMUNOELECTRON MICROSCOPE STUDYNeuropathology and Applied Neurobiology, 1981
- Reinvestigation of extremely acidic proteins in bovine brainBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Topographical distribution of fast and slow migrating fractions of beef brain S-100 protein fractionLife Sciences, 1968
- A soluble protein characteristic of the nervous systemBiochemical and Biophysical Research Communications, 1965
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*Annals of the New York Academy of Sciences, 1964