Identification of a tyrosine residue in the saccharide binding site of ricin B-chain using N-[14C]acetylimidazole

Edward J. Wawrzynczak, Anna Falasca, William A. Jeffery, Graham J. Watson, Philip E. Thorpe

Research output: Contribution to journalArticle

2 Scopus citations

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 languageEnglish (US)
Pages (from-to)51-55
Number of pages5
JournalFEBS Letters
Volume219
Issue number1
DOIs
StatePublished - 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

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