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Radiation research1968; 36(1); 22-30;

The binding of plutonium to serum proteins in vitro.

Abstract: The interactions between tetravalent plutonium and horse serum proteins were studied in vitro by electrophoresis on cellulose acetate and by gel filtration. The results show that in horse serum, as in other mammalian sera, the plutonium is associated principally with the transferrin component of the beta1-globulins. The formation of the plutonium-transferrin complex requires the presence of HCO3-, and plutonium is displaced from the complex by excess iron, thus indicating that similar binding sites may be involved in the complexing of iron and plutonium. The plutonium complex is considered to be less stable than the iron-transferrin complex, but plutonium can only be released from the transferrin complex by citrate or stronger chelating agents.
Publication Date: 1968-10-01 PubMed ID: 17387923
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study investigates how the radioactive element plutonium binds to proteins found in horse serum in a laboratory setting. The primary finding is that in horse serum, as in other mammal’s blood serum, plutonium chiefly binds to the transferrin component of the protein group called beta1-globulins.

Research Methodology

The researchers used two main techniques to explore the interaction between plutonium and horse serum proteins, which were electrophoresis on cellulose acetate and gel filtration.

  • Electrophoresis on cellulose acetate: This is a technique used to separate proteins based on their size, shape, and charge. In this case, it was used to observe where the plutonium was binding on the proteins.
  • Gel filtration: Also known as size exclusion chromatography, this method also separates proteins, but it does so according to their size. The researchers utilized this method to verify the results obtained from the electrophoresis.

Key Findings

The main findings of this study can be broken down into several significant points:

  • The plutonium in the horse serum principally binds with the transferrin component of the beta1-globulins proteins.
  • Creating the plutonium-transferrin complex requires the presence of HCO3-, bicarbonate ions. This suggests that bicarbonate ions play a role in the binding process.
  • Plutonium can be pushed out of the complex if there is an excess amount of iron. This implies that the binding sites for iron and plutonium could be similar, or indeed the same.
  • The stability of the plutonium-transferrin complex is less than that of the iron-transferrin complex. However, the plutonium can only be removed from the complex by the use of citrate or other stronger chelating agents, revealing the substantial binding strength of the plutonium to the transferrin protein.

In simplifying this process, the researchers have found that plutonium binds with the transferrin, a protein in horse serum, in a similar way it binds with other mammalian blood serum proteins.

Cite This Article

APA
Turner GA, Taylor DM. (1968). The binding of plutonium to serum proteins in vitro. Radiat Res, 36(1), 22-30.

Publication

ISSN: 0033-7587
NlmUniqueID: 0401245
Country: United States
Language: English
Volume: 36
Issue: 1
Pages: 22-30

Researcher Affiliations

Turner, G A
  • Department of Biophysics, Institute of Cancer Research, Belmont, Sutton, Surrey, England.
Taylor, D M

    MeSH Terms

    • Animals
    • Binding Sites
    • Blood Proteins / chemistry
    • Horses
    • Kinetics
    • Plutonium / chemistry
    • Protein Binding
    • Transferrin / chemistry

    Citations

    This article has been cited 1 times.
    1. Szot Z, Rochalska M, Wojewódzka M, Chimiak A, Przychodzen W. Removal of 239Pu from mice with 3,4,3 LICAM(C) or N,N',N'',N'''-tetra-(2,3-dihydroxybenzoyl)-spermine.. Radiat Environ Biophys 1986;25(1):31-5.
      doi: 10.1007/BF01209682pubmed: 3754971google scholar: lookup