Intramitochondrial localization of kynurenine aminotransferase.
نویسندگان
چکیده
Comparisons with the distribution of intramitochondrial marker enzymes have indicated that kynurenine aminotransferase is present in the inner membrane fraction of rat liver mitochondria. It appears to be weakly bound to the inner membrane because it is easily solubilized by increasing the concentration of digitonin. With the use of a-ketoglutarate or oxalacetate as amino group acceptor, the aminotransferase has been found to transaminate 3-hydroxy-Lkynurenine as well as L-kynurenine.
منابع مشابه
Enzymatic Properties of the Inner and Outer Membranes of Rat Liver Mitochondria
Treatment of rat liver mitochondria with digitonin followed by differential centrifugation was used to resolve the intramitochondrial localization of both soluble and particulate enzymes. Rat liver mitochondria were separated into three fractions: inner membrane plus matrix, outer membrane, and a soluble fraction containing enzymes localized between the membranes plus some solublized outer memb...
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The present study describes the isolation of a protein from Escherichia coli possessing kynurenine aminotransferase (KAT) activity and its identification as aspartate aminotransferase (AspAT). KAT catalyses the transamination of kynurenine and 3-hydroxykynurenine to kynurenic acid and xanthurenic acid respectively, and the enzyme activity can be easily detected in E. coli cells. Separation of t...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 245 14 شماره
صفحات -
تاریخ انتشار 1970