Genetic construction of a phosphorylation site in ricin A chain: specific radiolabeling of recombinant proteins for localization and degradation studies

Biochem Biophys Res Commun. 1995 May 16;210(2):253-9. doi: 10.1006/bbrc.1995.1654.

Abstract

Ricin A chain was modified by the addition of the heptapeptide LRRASLG (Kemptide) and a histidine tag for bacterial expression. The mutagenized toxin was purified by nickel column and could be phosphorylated in vitro by protein kinase A as demonstrated by labeling with [gamma-32P] ATP. Kemptide-A chain could be labeled even after reassociation with ricin B chain or disulfide linkage to antibody to form an immunotoxin. The 32P label in all cases was associated only with the A chain; ricin B chain and antibody were not kinase substrates alone or after conjugation. Kemptide-immunotoxin was tested in cytotoxicity assays and used to monitor internalization of the toxin moiety after [32P] phosphorylation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, Affinity
  • Histidine / chemistry
  • Hydrolysis
  • Molecular Sequence Data
  • Oligopeptides / chemistry
  • Phosphorus Radioisotopes
  • Phosphorylation
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Ricin / genetics
  • Ricin / isolation & purification
  • Ricin / metabolism*

Substances

  • Oligopeptides
  • Phosphorus Radioisotopes
  • Recombinant Proteins
  • Histidine
  • kemptide
  • Ricin