Abstract
Abstract: Two major components of human brain S100 fraction were purified by HPLC and an amino acid sequence was elucidated for the S100β component. Human S100 proteins showed absorption spectra and amino acid compositions similar to S100α and S100β from bovine brain. However, the relative amounts of the human proteins were 4% S100α and 96% S100β by weight, while the bovine protein distribution was 47% S100α and 53% S100β by weight. An amino acid sequence of human S100β was established by analysis of overlapping fragments generated by cyanogen bromide and trypsin cleavage. Three amino acid sequence differences between the human and bovine S100β were found at residues 7, 62, and 80. These differences were chemically conservative and compatible with minimum single base changes in the codon structures. These results document that S100β is a conserved protein among mammals and provide the necessary foundation for current clinical studies.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 700-705 |
| Number of pages | 6 |
| Journal | Journal of neurochemistry |
| Volume | 45 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 1985 |
Keywords
- Amino acid sequence
- Calcium
- Protein purification
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
- Biochemistry