Interspecies comparison of cytosolic and mitochondrial aspartate aminotransferases. Evidence for a more conservative evolution of the mitochondrial isoenzyme.
The degree of structural similarity between the mitochondrial isoenzymes of aspartate aminotransferase from pig heart and chicken heart was determined by means of their immunological cross-reactivity and compared with the degree of similarity between the cytosolic isoenzymes from the same two species. Quantitative microcomplement fixation revealed a remarkable similarity of the two mitochondrial isoenzymes corresponding to an immunological distance of 104. The structures of the two cytosolic isoenzymes, on the other hand, diverge with an immunological distance of 203. The apparent conservatism of mitochondrial aspartate aminotransferase indicates additional evolutionary constraints on the structure of this organelle-confined isoenzyme.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000276:immunology / Q000378:metabolism*; D005075:Biological Evolution; D002645:Chickens; D003168:Complement Fixation Tests; D003429:Cross Reactions; D003600:Cytosol / Q000201:enzymology*; D005779:Immunodiffusion; D007527:Isoenzymes / Q000378:metabolism*; D008931:Mitochondria, Muscle / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine
D007527:Isoenzymes; D001219:Aspartate Aminotransferases