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Bovine brain S100 proteins: separation and characterization of a new S100 protein species.
- Source :
-
Journal of neurochemistry [J Neurochem] 1983 Jan; Vol. 40 (1), pp. 145-52. - Publication Year :
- 1983
-
Abstract
- Three S100 protein species (S100a, S100b, S100a') have been purified from bovine brain using a modification of standard preparative methods. A higher yield for each protein was obtained at the last separation step. Characterization by urea/sodium dodecyl sulfate/polyacrylamide gel electrophoresis, UV absorption spectra, and fluorescence parameters provided evidence of a new tryptophan-containing S100 protein called S100a', which exhibits, as S100a and S100b, the properties of a Ca2+ binding protein.
- Subjects :
- Animals
Calcium
Cattle
Chromatography, Gel
Chromatography, Ion Exchange
Immunodiffusion
Molecular Weight
Nerve Growth Factors
Peptide Fragments analysis
S100 Calcium Binding Protein beta Subunit
Spectrophotometry, Ultraviolet
Biomarkers
Brain Chemistry
Nerve Tissue Proteins isolation & purification
S100 Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0022-3042
- Volume :
- 40
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of neurochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6401321
- Full Text :
- https://doi.org/10.1111/j.1471-4159.1983.tb12664.x