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. 1973 Mar;70(3):909–913. doi: 10.1073/pnas.70.3.909

Inactive Enzyme Molecules in Aging Mice: Liver Aldolase

Harriet Gershon 1, David Gershon 1
PMCID: PMC433386  PMID: 4197629

Abstract

Evidence is presented that there is a considerable accumulation of inactive fructose-1,6-diphosphate aldolase (EC 4.1.2.7) in the liver of senescent mice. Liver aldolase was purified from 3-month-old mice and used to immunize rabbits. It was demonstrated with the monospecific antibody thus produced that the liver aldolase of young adult (3 month) and aged (31 month) mice are antigenically identical. With the antibody, inactive enzyme molecules (crossreacting material) in liver homogenate of old mice were detected. The liver aldolase of senescent mice had half as much active enzyme per mg of protein, as well as per antigenic unit, as did the liver aldolase of young adult mice. The accumulation of faulty enzyme molecules may be one of the causes of debilitation leading to senescence and death.

Keywords: senescence; fructose-1,6-diphosphate aldolase

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Selected References

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

  1. Fornaini G., Leoncini G., Segni P., Calabria G. A., Dachà M. Relationship between age and properties of human and rabbit erythrocyte glucose-6-phosphate dehydrogenase. Eur J Biochem. 1969 Jan;7(2):214–222. doi: 10.1111/j.1432-1033.1969.tb19594.x. [DOI] [PubMed] [Google Scholar]
  2. Gershon H., Gershon D. Detection of inactive enzyme molecules in ageing organisms. Nature. 1970 Sep 19;227(5264):1214–1217. doi: 10.1038/2271214a0. [DOI] [PubMed] [Google Scholar]
  3. Gracy R. W., Lacko A. G., Brox L. W., Adelman R. C., Horecker B. L. Structural relations in aldolases purified from rat liver and muscle and Novikoff hepatoma. Arch Biochem Biophys. 1970 Feb;136(2):480–490. doi: 10.1016/0003-9861(70)90219-5. [DOI] [PubMed] [Google Scholar]
  4. Gracy R. W., Lacko A. G., Horecker B. L. Subunit structure and chemical properties of rabbit liver aldolase. J Biol Chem. 1969 Jul 25;244(14):3913–3919. [PubMed] [Google Scholar]
  5. Holliday R. Errors in protein synthesis and clonal senescence in fungi. Nature. 1969 Mar 29;221(5187):1224–1228. doi: 10.1038/2211224a0. [DOI] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Lewis C. M., Holliday R. Mistranslation and ageing in Neurospora. Nature. 1970 Nov 28;228(5274):877–880. doi: 10.1038/228877a0. [DOI] [PubMed] [Google Scholar]
  8. ORGEL L. E. The maintenance of the accuracy of protein synthesis and its relevance to ageing. Proc Natl Acad Sci U S A. 1963 Apr;49:517–521. doi: 10.1073/pnas.49.4.517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Palmer W. G., Papaconstantinou J. Aging of alpha-crystallins during development of the lens. Proc Natl Acad Sci U S A. 1969 Sep;64(1):404–410. doi: 10.1073/pnas.64.1.404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Penhoet E., Rajkumar T., Rutter W. J. Multiple forms of fructose diphosphate aldolase in mammalian tissues. Proc Natl Acad Sci U S A. 1966 Oct;56(4):1275–1282. doi: 10.1073/pnas.56.4.1275. [DOI] [PMC free article] [PubMed] [Google Scholar]

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