Abstract
The binding of ricin B-chain to Sepharose, a galactose-based adsorbent, was reversibly inactivated by acetylation of tyrosine residues in the absence of lactose. In the presence of lactose, two tyrosine residues were protected against modification and the B-chain retained its binding ability. Analyses of tryptic peptides from B-chain modified with N-[14C]acetylimidazole in the presence and absence of lactose showed that Tyr-248 is present in one of the galactose-binding sites.
Original language | English (US) |
---|---|
Pages (from-to) | 51-55 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 219 |
Issue number | 1 |
DOIs | |
State | Published - Jul 13 1987 |
Keywords
- B-chain
- N-[C]Acetylimidazole
- Ricin
- Saccharide binding
- Tyrosine residue
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology