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Inhibition by streptozotocin of the activity of succinyl‐Co A synthetase in vitro and in vivo
Author(s) -
Boquist L.,
Ericsson I.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80275-7
Subject(s) - streptozotocin , in vivo , in vitro , endocrinology , medicine , diabetes mellitus , kidney , enzyme , chemistry , biology , biochemistry , microbiology and biotechnology
The activity of succinyl‐CoA synthetase from mouse liver and kidney was inhibited by streptozotocin in vitro. Streptozotocin behaved essentially as a non‐competitive inhibitor, and the following kinetic values were obtained (in the presence of 10 nM streptozotocin): apparent K m 1.7 mM, apparent K i 10 nM, and k cat 440 nkat·kg −1 . Compared with non‐diabetic control mice, the succinyl‐CoA synthetase activity was significantly decreased in the islets and kidneys of mice with early (1 h) and manifest (≧ 2 days) streptozotocin diabetes, whereas the activity in the liver was not significantly altered. Inhibited succinyl‐CoA synthetase activity is believed to play a prominent role in the cellular effects of streptozotocin.