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Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents.

Publication ,  Journal Article
Vaidyanathan, G; Zalutsky, MR
Published in: Bioconjug Chem
1990

In previous studies we have demonstrated that antibodies radioiodinated with N-succinimidyl 3-iodobenzoate (SIB) are less susceptible to loss of radioiodine in vivo than antibodies iodinated directly by electrophilic substitution on their tyrosine residues with Iodogen. Since the Bolton-Hunter reagent, N-succinimidyl 3-(4-hydroxy-3-iodophenyl)propionate, is identical with SIB except that it contains a hydroxyl group on the aromatic ring and a two-methylene spacer, a comparison of their coupling chemistry and in vivo behavior was performed to better understand the structural requirements for a useful iodinated acylation agent. Protein concentration and pH had a significant effect on the coupling efficiency of both SIB and the Bolton-Hunter reagent; however, protein-labeling yields with SIB were generally higher by a factor of 2. Paired-label biodistribution studies in mice demonstrated that thyroid uptake (a monitor of dehalogenation) of antibody labeled by the Bolton-Hunter method was twice that of antibody labeled with SIB but only 7% of that observed for antibody labeled with Iodogen. These results suggest that even minor differences in iodination site can profoundly alter the retention of label on a protein in vivo.

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Published In

Bioconjug Chem

DOI

ISSN

1043-1802

Publication Date

1990

Volume

1

Issue

4

Start / End Page

269 / 273

Location

United States

Related Subject Headings

  • Tissue Distribution
  • Thyroid Gland
  • Succinimides
  • Proteins
  • Organic Chemistry
  • Mice
  • Iodobenzoates
  • Iodine Radioisotopes
  • Goats
  • Antibodies, Monoclonal
 

Citation

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Vaidyanathan, G., & Zalutsky, M. R. (1990). Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents. Bioconjug Chem, 1(4), 269–273. https://doi.org/10.1021/bc00004a007
Vaidyanathan, G., and M. R. Zalutsky. “Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents.Bioconjug Chem 1, no. 4 (1990): 269–73. https://doi.org/10.1021/bc00004a007.
Vaidyanathan G, Zalutsky MR. Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents. Bioconjug Chem. 1990;1(4):269–73.
Vaidyanathan, G., and M. R. Zalutsky. “Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents.Bioconjug Chem, vol. 1, no. 4, 1990, pp. 269–73. Pubmed, doi:10.1021/bc00004a007.
Vaidyanathan G, Zalutsky MR. Protein radiohalogenation: observations on the design of N-succinimidyl ester acylation agents. Bioconjug Chem. 1990;1(4):269–273.
Journal cover image

Published In

Bioconjug Chem

DOI

ISSN

1043-1802

Publication Date

1990

Volume

1

Issue

4

Start / End Page

269 / 273

Location

United States

Related Subject Headings

  • Tissue Distribution
  • Thyroid Gland
  • Succinimides
  • Proteins
  • Organic Chemistry
  • Mice
  • Iodobenzoates
  • Iodine Radioisotopes
  • Goats
  • Antibodies, Monoclonal