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Clinical Chemistry 36: 687-689, 1990;
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Clinical Chemistry, Vol 36, 687-689, Copyright © 1990 by American Association for Clinical Chemistry

New automated measurement of mitochondrial aspartate aminotransferase with use of protease 401

Y Watazu, Y Uji, H Sugiuchi, H Okabe and S Murao
Department of Laboratory Medicine, Kumamoto University Medical School, Japan.

Total mitochondrial aspartate aminotransferase (EC 2.6.1.1), the sum of apo- and holo-mitochondrial aspartate aminotransferase activity in human serum, was measured by using a proteolytic method: inactivation of cytosolic aspartate aminotransferase with cytosolic aspartate aminotransferase-inactivating protease 401 from Streptomyces violaceochromogenes. Cytosolic aspartate aminotransferase is completely inactivated, and apo-mitochondrial aspartate aminotransferase is completely activated by pyridoxal 5'-phosphate within 5 min. Results by the proposed method correlated well with those by an immunochemical method (r = 0.994, n = 145) and showed excellent inhibitory activity of the protease for holo- and apo-cytosolic aspartate aminotransferase up to 5000 U/L and activation of mitochondrial apo-aspartate aminotransferase up to 2000 U/L in the presence of 100 mumol of pyridoxal 5'-phosphate per liter. Within-run Cvs were good (1.13- 7.49%). Mean values for total mitochondrial aspartate aminotransferase and apo-mitochondrial aspartate aminotransferase activities in serum of the healthy subjects were 4.8 (SD 0.9) and 1.8 (SD 0.8) U/L, respectively (n = 154). Various common interferents tested did not affect this assay.




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Copyright © 1990 by the American Association for Clinical Chemistry.