Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1968 Jul;108(4):619–624. doi: 10.1042/bj1080619

Two forms of aspartate aminotransferase in rat liver and kidney mitochondria

M M Bhargava 1, A Sreenivasan 1
PMCID: PMC1198859  PMID: 5667274

Abstract

1. Butan-1-ol solubilizes that portion of rat liver mitochondrial aspartate aminotransferase (EC 2.6.1.1) that cannot be solubilized by ultrasonics and other treatments. 2. A difference in electrophoretic mobilities, chromatographic behaviour and solubility characteristics between the enzymes solubilized by ultrasonic treatment and by butan-1-ol was observed, suggesting the occurrence of two forms of this enzyme in rat liver mitochondria. 3. Half the aspartate aminotransferase activity of rat kidney homogenate was present in a high-speed supernatant fraction, the remainder being in the mitochondria. 4. A considerable increase in aspartate aminotransferase activity was observed when kidney mitochondrial suspensions were treated with ultrasonics or detergents. 5. All the activity after maximum activation was recoverable in the supernatant after centrifugation at 105000g for 1hr. 6. The electrophoretic mobility of the kidney mitochondrial enzyme was cathodic and that of the supernatant enzyme anodic. 7. Cortisone administration increased the activities of both mitochondrial and supernatant aspartate aminotransferases of liver, but only that of the supernatant enzyme of kidney.

Full text

PDF
619

Selected References

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

  1. BOYD J. W. The intracellular distribution, latency and electrophoretic mobility of L-glutamate-oxaloacetate transaminase from rat liver. Biochem J. 1961 Nov;81:434–441. doi: 10.1042/bj0810434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bhargava M. M., Sreenivasan A. On the binding of rat liver aspartate amino transferase on the mitochondrial membrane. Enzymologia. 1966 Nov 30;31(5):262–266. [PubMed] [Google Scholar]
  3. Bhargava M. M., Sreenivasan A. On the origin of increased serum aspartate amino transferase in hepatic damage. Enzymologia. 1966 Oct 31;31(4):245–249. [PubMed] [Google Scholar]
  4. Boyd J. W. The extraction and purification of two isoenzymes of L-aspartate:2-oxoglutarate aminotransferase. Biochim Biophys Acta. 1966 Feb 14;113(2):302–311. doi: 10.1016/s0926-6593(66)80069-3. [DOI] [PubMed] [Google Scholar]
  5. DECKER L. E., RAU E. M. Multiple forms of glutamic-oxalacetic transaminase in tissues. Proc Soc Exp Biol Med. 1963 Jan;112:144–149. doi: 10.3181/00379727-112-27975. [DOI] [PubMed] [Google Scholar]
  6. EICHEL H. J., BUKOVSKY J. Intracellular distribution pattern of rat liver glutamic-oxalacetic transaminase. Nature. 1961 Jul 15;191:243–245. doi: 10.1038/191243a0. [DOI] [PubMed] [Google Scholar]
  7. ESTRADA S., CORDOBA F. CORTISOL ACTIVATION OF RAT LIVER GLUTAMATEASPARTATE TRANSAMINASE. Biochem Biophys Res Commun. 1963 Aug 20;12:487–491. doi: 10.1016/0006-291x(63)90321-8. [DOI] [PubMed] [Google Scholar]
  8. GAVOSTO F., PILERI A., BRUSCA A. Increased transaminase activity in the liver after administration of cortisone. Biochim Biophys Acta. 1957 May;24(2):250–254. doi: 10.1016/0006-3002(57)90190-7. [DOI] [PubMed] [Google Scholar]
  9. GOLDSTEIN L., STELLA E. J., KNOX W. E. The effect of hydrocortisone on tyrosine-alpha-ketoglutarate transaminase and tryptophan pyrrolase activities in the isolated, perfused rat liver. J Biol Chem. 1962 May;237:1723–1726. [PubMed] [Google Scholar]
  10. Hirschberg E., Snider D., Osnos M. Effect of changes in hormonal and dietary status of rats and mice on the activity of their liver glutamic dehydrogenases. Adv Enzyme Regul. 1964;2:301–310. doi: 10.1016/s0065-2571(64)80021-2. [DOI] [PubMed] [Google Scholar]
  11. KENNEY F. T. Induction of tyrosine-alpha-ketoglutarate transaminase in rat liver. IV. Evidence for an increase in the rate of enzyme synthesis. J Biol Chem. 1962 Nov;237:3495–3498. [PubMed] [Google Scholar]
  12. Martinez-Carrion M., Riva F., Turano C., Fasella P. Multiple forms of supernatant glutamate-aspartate transaminase from pig heart. Biochem Biophys Res Commun. 1965 Jul 12;20(2):206–211. doi: 10.1016/0006-291x(65)90347-5. [DOI] [PubMed] [Google Scholar]
  13. ROBERTS N. R., ROSEN F., BUDNICK L. E., NICHOL C. A. An enzymatic basis for the gluconeogenic action of hydrocortisone. Science. 1958 Feb 7;127(3293):287–288. doi: 10.1126/science.127.3293.287-b. [DOI] [PubMed] [Google Scholar]
  14. SEGAL H. L., ROSSO R. G., HOPPER S., WEBER M. M. Direct evidence for an increase in enzyme level as the basis for the glucocorticoid-induced increase in glutamic-alanine transaminase activity in rat liver. J Biol Chem. 1962 Oct;237:PC3303–PC3305. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES