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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Jan;81(1):150–154. doi: 10.1073/pnas.81.1.150

Radiation inactivation of oligomeric enzyme systems: theoretical considerations.

A S Verkman, K Skorecki, D A Ausiello
PMCID: PMC344628  PMID: 6582472

Abstract

Radiation inactivation has been used as a tool to explore the size, structure, and function of soluble and membrane-bound enzymes. Enzyme systems consisting of a single functional unit yield a single exponential dependence of enzyme activity on radiation dose. Complex, nonexponential, inactivation curves suggest the presence of a multiunit enzyme system. A concave-upward inactivation curve suggests the presence of multiple independent functional units of distinct size and activity that do not interact with each other. An oligomeric enzyme, consisting of n identical subunits in equilibrium with monomers, can give simple exponential decay curves or more complex inactivation curves with various degrees of upward or downward concavity, depending upon the extent of oligomer-monomer equilibration among subunits after radiation, oligomer-to-monomer size and activity ratios, and multihit requirements for oligomer inactivation. For each of these possibilities, equations for the inactivation curves are derived, calculated numerically, and discussed in qualitative terms. A systematic approach to the evaluation of complex radiation inactivation curves is proposed and limitations of the radiation inactivation method are reviewed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blum E., Alper T. Radiation-target molecular weights of urease and of L-glutamate dehydrogenase, and their relevance to the size of the functional subunits. Biochem J. 1971 May;122(5):677–680. doi: 10.1042/bj1220677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Green F. A., Jung C. Y., Cuppoletti J., Owens N. Hypertonic cryohemolysis and the cytoskeletal system. Biochim Biophys Acta. 1981 Nov 6;648(2):225–230. doi: 10.1016/0005-2736(81)90038-9. [DOI] [PubMed] [Google Scholar]
  3. Harmon J. T., Kahn C. R., Kempner E. S., Schlegel W. Characterization of the insulin receptor in its membrane environment by radiation inactivation. J Biol Chem. 1980 Apr 25;255(8):3412–3419. [PubMed] [Google Scholar]
  4. Kempner E. S., Miller J. H., Schlegel W., Hearon J. Z. The functional unit of polyenzymes. Determination by radiation inactivation. J Biol Chem. 1980 Jul 25;255(14):6826–6831. [PubMed] [Google Scholar]
  5. Kempner E. S., Schlegel W. Size determination of enzymes by radiation inactivation. Anal Biochem. 1979 Jan 1;92(1):2–10. doi: 10.1016/0003-2697(79)90617-1. [DOI] [PubMed] [Google Scholar]
  6. Kincaid R. L., Kempner E., Manganiello V. C., Osborne J. C., Jr, Vaughan M. Calmodulin-activated cyclic nucleotide phosphodiesterase from brain. Relationship of subunit structure to activity assessed by radiation inactivation. J Biol Chem. 1981 Nov 10;256(21):11351–11355. [PubMed] [Google Scholar]
  7. Schlegel W., Kempner E. S., Rodbell M. Activation of adenylate cyclase in hepatic membranes involves interactions of the catalytic unit with multimeric complexes of regulatory proteins. J Biol Chem. 1979 Jun 25;254(12):5168–5176. [PubMed] [Google Scholar]
  8. Simon P., Swillens S., Dumont J. E. Size determination of an equilibrium enzymic system by radiation inactivation: theoretical considerations. Biochem J. 1982 Sep 1;205(3):477–483. doi: 10.1042/bj2050477. [DOI] [PMC free article] [PubMed] [Google Scholar]

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