Subcellular distribution of aspartate aminotransferase isoenzymes in chicken heart: quantitative study
- PMID: 7060345
- DOI: 10.1016/0305-0491(82)90239-5
Subcellular distribution of aspartate aminotransferase isoenzymes in chicken heart: quantitative study
Abstract
1. The content of the two aspartate aminotransferase isoenzymes in isolated mitochondria and in the cytosolic fraction from chicken heart was determined by radioimmunoassays. 2. The cationic isoenzyme was found to be associated with the mitochondrial fraction; its content measured in the cytosolic fraction was within the range of that of contaminating mitochondrial marker enzymes. 3. The anionic isoenzyme was found exclusively in the cytosolic fraction, in mitochondria a content of less than 0.05% of the total was measured. 4. Thus, in birds, the anionic and the cationic isoenzyme of aspartate aminotransferase show the same strict intracellular heterotopism as found previously in mammals.
Similar articles
-
Independent quantitation of the mitochondrial and the cytosolic isoenzyme of aspartate aminotransferase in chicken tissues by radioimmunoassays.J Biol Chem. 1981 Apr 10;256(7):3381-4. J Biol Chem. 1981. PMID: 7204406
-
Interspecies comparison of cytosolic and mitochondrial aspartate aminotransferases. Evidence for a more conservative evolution of the mitochondrial isoenzyme.J Biol Chem. 1977 Jan 25;252(2):609-12. J Biol Chem. 1977. PMID: 401816
-
Biosynthesis of aspartate aminotransferases. Both the higher molecular weight precursor of mitochondrial aspartate aminotransferase and the cytosolic isoenzyme are synthesized on free polysomes.J Biol Chem. 1982 Mar 25;257(6):3339-45. J Biol Chem. 1982. PMID: 7061479
-
Structural and genetic relationships between cytosolic and mitochondrial isoenzymes.Int J Biochem. 1984;16(12):1193-9. doi: 10.1016/0020-711x(84)90216-7. Int J Biochem. 1984. PMID: 6397370 Review.
-
Evolutionary and biosynthetic aspects of aspartate aminotransferase isoenzymes and other aminotransferases.Ann N Y Acad Sci. 1990;585:331-8. doi: 10.1111/j.1749-6632.1990.tb28065.x. Ann N Y Acad Sci. 1990. PMID: 2192617 Review.
Cited by
-
A homologue of the axonally secreted protein axonin-1 is an integral membrane protein of nerve fiber tracts involved in neurite fasciculation.J Cell Biol. 1989 Nov;109(5):2363-78. doi: 10.1083/jcb.109.5.2363. J Cell Biol. 1989. PMID: 2509484 Free PMC article.