Proteolytic measurement of mitochondrial aspartate aminotransferase in human serum

✍ Scribed by Yoshifumi Watazu; Hiroaki Okabe; Hiroyuki Sugiuchi; Yoshinori Uji; Yasushi Shirahase; Nobuaki Kaneda

• Publisher: Elsevier Science
• Year: 1990
• Tongue: English
• Weight: 309 KB
• Volume: 23
• Category: Article
• ISSN: 0009-9120
• DOI: 10.1016/0009-9120(90)80023-c

✦ Synopsis

A new proteolytic measurement of serum mitochondrial aspartate aminotransferase was evaluated using cytosolic aspartate aminotransferase inactivating protease. Some of the proteases, such as, c(-chymotrypsin, subtilisin and cytosolic aspartate aminotransferase inactivating protease 401 from Streptomyces species, also specifically inactivated cytosolic aspartate aminotransferase, but not mitochondrial aspar~ate aminotransferase]lThe protease 401 was the most heat stable for storage and showed a higher inactivation rate for cytosolic aspartate aminotransferase--up to 7000 lUlL--more than 200-fold the upper limit. The coefficient of variation of the proteolytic method was less than 10%. Results by the present method correlated with those by the immunochemical method (r= 0.970) and the regression curve was Y=0.95X+1.60 (Y: Immunochemical method; X: proteolytic method). In the present assay system, reference values for mitochondrial aspartate aminotransferase activity in 500 healthy people ranged from 2.0-7.2 U/L (mean 3.8 U/L).