Covalent attachment of metal chelates to proteins: the stability in vivo and in vitro of the conjugate of albumin with a chelate of 111indium

C. F. Meares, D. A. Goodwin, C. S H Leung, A. Y. Girgis, D. J. Silvester, A. D. Nunn, P. J. Lavender

Research output: Contribution to journalArticle

63 Scopus citations

Abstract

Human serum albumin has been conjugated to 1 (p benzenediazonium) ethylenedinitrilo) tetraacetic acid, a powerful chelating agent, and radioactive 111indium ions have been added specifically to the chelating groups. The product, with a specific radioactivity of about 1 mCi/mg of protein, was employed as a radiotracer in scintillation scanning studies with human volunteers. Results show that 48 hr after injection, practically all of the label remains attached to albumin. This is confirmed by electrophoresis of serum proteins; 7 days after injection, 85% of the radioactivity in the serum is still in the albumin fraction. These observations agree with in vitro studies of the labeled albumin in human serum, where loss of the metal ion from the chelating group to the protein transferrin amounts to less than 3% after 1 week and less than 5% after 2 weeks. Measurements of the distribution of label in mice up to 23 days after injection suggest that metabolism of the labeled protein does not lead to binding of indium ions by transferrin. The binding of indium and other metal ions by transferrin has previously posed a major impediment to the use of metal chelates for in vivo diagnostic procedures. Demonstration of the kinetic inertness of the chelate in these experiments suggests the use of related chelates as physical probes of biological systems.

Original languageEnglish (US)
Pages (from-to)3803-3806
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume73
Issue number11
StatePublished - 1976

ASJC Scopus subject areas

  • Genetics
  • General

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