Open AccessOptimal conditions for protease use in the assay of serum mitochondrial aspartate aminotransferase
Author(s) -
Okabe Hiroaki,
Uji Yoshinori,
Sugiuchi Hiroyuki,
Watazu Yoshifumi,
Shirahase Yasushi,
Kaneda Nobuaki
Publication year - 1990
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.1860040507
Subject(s) - protease , biochemistry , alanine aminotransferase , chemistry , enzyme , biology , endocrinology
Abstract 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 reagent 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 aα 1 ‐antitrypsin and α 2 ‐macroglobin did not inhibit protease 401.