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. 1970 Sep;119(2):157–160. doi: 10.1042/bj1190157

Haem a, cytochrome c and total protein turnover in mitochondria from rat heart and liver

V Aschenbrenner 1, R Druyan 1, R Albin 1, M Rabinowitz 1
PMCID: PMC1179336  PMID: 5488910

Abstract

Haem a and cytochrome c were isotopically labelled in mitochondria from rat heart and liver after injection of δ-amino[2,3-3H2]laevulate, a specific haem precursor. [guanido-14C]Arginine or l-[4,5-3H2]leucine were used to label mitochondrial proteins. Half-lives were measured from biological decay in vivo and were similar (5.5–6.2 days) for haem a, cytochrome c and [14C]arginine-labelled proteins. Labelling of hepatic mitochondrial proteins with [3H2]leucine resulted in a prolonged apparent half-life.

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Selected References

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

  1. Beattie D. S. The turnover of the protein components of the inner and outer membrane fractions of rat liver mitochondria. Biochem Biophys Res Commun. 1969 Jun 6;35(5):721–727. doi: 10.1016/0006-291x(69)90465-3. [DOI] [PubMed] [Google Scholar]
  2. Brunner G., Neupert W. Turnover of outer and inner membrane proteins of rat liver mitochondria. FEBS Lett. 1968 Aug;1(3):153–155. doi: 10.1016/0014-5793(68)80045-6. [DOI] [PubMed] [Google Scholar]
  3. CONNELLY J. L., MORRISON M., STOTZ E. Hemins of beef heart muscle. J Biol Chem. 1958 Sep;233(3):743–747. [PubMed] [Google Scholar]
  4. Druyan R., DeBernard B., Rabinowitz M. Turnover of cytochromes labeled with delta-aminolevulinic acid-3H in rat liver. J Biol Chem. 1969 Nov 10;244(21):5874–5878. [PubMed] [Google Scholar]
  5. FLETCHER M. J., SANADI D. R. Turnover of rat-liver mitochondria. Biochim Biophys Acta. 1961 Aug 5;51:356–360. doi: 10.1016/0006-3002(61)90177-9. [DOI] [PubMed] [Google Scholar]
  6. Gross N. J., Getz G. S., Rabinowitz M. Apparent turnover of mitochondrial deoxyribonucleic acid and mitochondrial phospholipids in the tissues of the rat. J Biol Chem. 1969 Mar 25;244(6):1552–1562. [PubMed] [Google Scholar]
  7. 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]
  8. Levin W., Kuntzman R. Biphasic decrease of radioactive hemoprotein from liver microsomal CO-binding particles. Effect of 3-methylcholanthrene. J Biol Chem. 1969 Jul 10;244(13):3671–3676. [PubMed] [Google Scholar]
  9. MARGOLIASH E., FROHWIRT N., WIENER E. A study of the cytochrome c haemochromogen. Biochem J. 1959 Mar;71(3):559–570. doi: 10.1042/bj0710559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. McKay R., Druyan R., Getz G. S., Rabinowitz M. Intramitochondrial localization of delta-aminolaevulate synthetase and ferrochelatase in rat liver. Biochem J. 1969 Sep;114(3):455–461. doi: 10.1042/bj1140455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. RAWLINSON W. A., HALE J. H. Prosthetic groups of the cytochromes present in Corynebacterium diphtheriae with especial reference to cytochrome a. Biochem J. 1949;45(3):247-55, pl. doi: 10.1042/bj0450247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. SILVERSTEIN E., BOYER P. D. EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF LIVER AND YEAST ALCOHOL DEHYDROGENASE. J Biol Chem. 1964 Nov;239:3908–3914. [PubMed] [Google Scholar]
  13. Schimke R. T., Ganschow R., Doyle D., Arias I. M. Regulation of protein turnover in mammalian tissues. Fed Proc. 1968 Sep-Oct;27(5):1223–1230. [PubMed] [Google Scholar]
  14. Swick R. W., Rexroth A. K., Stange J. L. The metabolism of mitochondrial proteins. 3. The dynamic state of rat liver mitochondria. J Biol Chem. 1968 Jul 10;243(13):3581–3587. [PubMed] [Google Scholar]
  15. Tschudy D. P., Marver H. S., Collins A. A model for calculating messenger RNA half-life: short lived messenger RNA in the induction of mammalian delta-aminolevulinic acid synthetase. Biochem Biophys Res Commun. 1965 Dec 9;21(5):480–487. doi: 10.1016/0006-291x(65)90408-0. [DOI] [PubMed] [Google Scholar]
  16. York J. L., McCoy S., Taylor D. N., Caughey W. S. Heme A of cytochrome c oxidase. I. Isolation from bovine heart. J Biol Chem. 1967 Mar 10;242(5):908–911. [PubMed] [Google Scholar]
  17. Zak R., Grove D., Rabinowitz M. DNA synthesis in the rat diaphragm as an early response to denervation. Am J Physiol. 1969 Mar;216(3):647–654. doi: 10.1152/ajplegacy.1969.216.3.647. [DOI] [PubMed] [Google Scholar]

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