Abstract
In rapidly frozen livers from chickens affected with myeloblastosis and Marek's disease and from unaffected control birds there exists a strong correlation between catalase activity and catalase Electron Paramagnetic Resonance (EPR) signal intensities. The diseased chickens had activities and signals reduced to as little as 10% of control values. There were no changes in the EPR parameters in diseased liver and the data support the hypothesis that the lowering in activity is due to lowered catalase levels rather than to catalase inhibition. The rate of transformation of catalase to catalase-formate in liver was studied by freeze-clamping liver in anaesthetised chickens, then warming to 37 degrees for 1 or 2 minutes anaerobiosis, and then refreezing. The only difference of significance in this transformation between diseased and normal livers was the greater percentage of total catalase present as catalase-formate (approximately + 15%) in aerobic diseased liver, which may indicate a lowered production of hydrogen peroxide, relative to formate, in these livers. The rate of transformation was far faster in chickens (t1/2 less than 1 min) than in the rat (t1/2 = 7.7 min).
Full text
PDF






Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BLASCHKO H., HAGEN J. M., HAGEN P. Mitochondrial enzymes and chromaffin granules. J Physiol. 1957 Dec 3;139(2):316–322. doi: 10.1113/jphysiol.1957.sp005893. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CERIOTTI G., SPANDRIO L., AGRADI A. A study of the synthesis of catalase in liver of tumor-bearing mice by means of radioactive iron. Biochim Biophys Acta. 1958 Feb;27(2):432–433. doi: 10.1016/0006-3002(58)90365-2. [DOI] [PubMed] [Google Scholar]
- Churchill A. E. Herpes-type virus isolated in cell culture from tumors of chickens with Marek's disease. I. Studies in cell culture. J Natl Cancer Inst. 1968 Oct;41(4):939–950. [PubMed] [Google Scholar]
- De Duve C., Baudhuin P. Peroxisomes (microbodies and related particles). Physiol Rev. 1966 Apr;46(2):323–357. doi: 10.1152/physrev.1966.46.2.323. [DOI] [PubMed] [Google Scholar]
- Dionisi O., Galeotti T., Terranova T., Azzi A. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochim Biophys Acta. 1975 Oct 22;403(2):292–300. doi: 10.1016/0005-2744(75)90059-5. [DOI] [PubMed] [Google Scholar]
- HARGREAVES A. B., DEUTSCH H. F. The in vitro inhibition of catalase by a tumor factor. Cancer Res. 1952 Oct;12(10):720–726. [PubMed] [Google Scholar]
- HARGREAVES A. B., LOBO L. C., CALMON LEMME C., HASSON A. In vitro and in vivo inhibition of catalase by uric acid and other nucleic acid catabolites. Cancer Res. 1959 Jun;19(5):468–471. [PubMed] [Google Scholar]
- KAMPSCHMIDT R. F. MECHANISM OF LIVER CATALASE DEPRESSION IN TUMOR-BEARING ANIMALS: A REVIEW. Cancer Res. 1965 Jan;25:34–45. [PubMed] [Google Scholar]
- NICHOLLS P. The action of anions on catalase peroxide compounds. Biochem J. 1961 Nov;81:365–374. doi: 10.1042/bj0810365. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NICHOLLS P. The formation and properties of sulphmyoglobin and sulphcatalase. Biochem J. 1961 Nov;81:374–383. doi: 10.1042/bj0810374. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NISHIMURA E. T., KOBARA T. Y., KALTENBACH J. P., WARTMAN W. B. Immunological evidence of repressed catalase synthesis in livers of tumor-bearing mice. Arch Biochem Biophys. 1962 Jun;97:589–595. doi: 10.1016/0003-9861(62)90128-5. [DOI] [PubMed] [Google Scholar]
- Oshino N., Chance B., Sies H., Bücher T. The role of H 2 O 2 generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors. Arch Biochem Biophys. 1973 Jan;154(1):117–131. doi: 10.1016/0003-9861(73)90040-4. [DOI] [PubMed] [Google Scholar]
- Oshino N., Jamieson D., Chance B. The properties of hydrogen peroxide production under hyperoxic and hypoxic conditions of perfused rat liver. Biochem J. 1975 Jan;146(1):53–65. doi: 10.1042/bj1460053. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PRICE V. E., GREENFIELD R. E. Liver catalase. II. Catalase fractions from normal and tumor-bearing rats. J Biol Chem. 1954 Jul;209(1):363–376. [PubMed] [Google Scholar]
- SAHA A., CAMPBELL D. H., SCHROEDER W. A. IMMUNOCHEMICAL STUDIES ON LIVER AND ERYTHROCYTE CATALASES FROM CATTLE, HORSE, RABBIT AND HUMAN. Biochim Biophys Acta. 1964 Apr 6;85:38–49. doi: 10.1016/0926-6569(64)90165-8. [DOI] [PubMed] [Google Scholar]
- Thamm R., Rapoport S., Nieradt-Hiebsch C. Uber die CO 2 -Bildung aus dem C 1 -Stoffwechsel von Aszites-Tumorzellen. Acta Biol Med Ger. 1971;27(3):459–476. [PubMed] [Google Scholar]
- Williams-Smith D. L., Morrison P. J. Electron paramagnetic resonance spectra of catalase in mammalian tissues. Biochim Biophys Acta. 1975 Oct 20;405(2):253–261. doi: 10.1016/0005-2795(75)90092-6. [DOI] [PubMed] [Google Scholar]
- Williams-Smith D. L., Patel K. Induced changes in the electron paramagnetic resonance spectra of mammalian catalases. Biochim Biophys Acta. 1975 Oct 20;405(2):243–252. doi: 10.1016/0005-2795(75)90091-4. [DOI] [PubMed] [Google Scholar]
- Yamanaka N., Deamer D. Superoxide dismutase activity in WI-38 cell cultures: effects of age, trypsinization and SV-40 transformation. Physiol Chem Phys. 1974;6(2):95–106. [PubMed] [Google Scholar]
