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Optimal conditions for protease use in the assay of serum mitochondrial aspartate aminotransferase

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

Publisher: John Wiley and Sons
Year: 1990
Tongue: English
Weight: 331 KB
Volume: 4
Category: Article
ISSN: 0887-8013
DOI: 10.1002/jcla.1860040507

No coin nor oath required. For personal study only.

✦ Synopsis

The optimal conditions for selective proteolytic inactivation of cytosolic aspartate aminotransferase (c-AST) to determine mitochondrial aspartate aminotransferase (m-AST) in serum were studied. Protease 401 was found to be effective over a pH range of 6.0-10.0. A pH of 9.5 with 0.5% albumin in the re-Key words: agent mixture was determined to be optimal for inactivation of c-AST and preservation of m-AST, lactic dehydrogenase (LDH), and malic dehydrogenase (MDH) in the assay procedure. The presence of serum endogenous protein inhibitors such as a,-antitrypsin and a,-macroglobin did not inhibit protease 401.

Aspartate aminotransferase isozyme, mitochondrial aspartate aminotransferase, cytosolic aspartate aminotransferase, proteolytic measurement, selective proteolysis, protease 401

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