منابع مشابه
Transaminase Activity in Neurospora crassa
It is now believed that the amino groups of isoleucine and valine are accepted by their respective carbon chains during biosynthesis via a transamination. Most of the evidence for this hypothesis has been derived from experiments on isoleucineless and valineless mutants of Escherichia coli and Neurospora crassu (l-4). It is not positively established whether this transamination step can be medi...
متن کاملThe Kynurenine Transaminase of Rat Kidney*
The conversion of kynurenine to kynurenic acid was observed in intact animals by Kotake (2) in 1931. This reaction was studied in vitro by Mason and Berg (3, 4), who observed that slices and homogenates of rat liver converted both tryptophan and kynurenine to kynurenic acid. Similar preparations from rat kidney did not convert tryptophan to kynurenine or kynurenic acid, but had a somewhat great...
متن کاملThe kynurenine transaminase of rat kidney.
The conversion of kynurenine to kynurenic acid was observed in intact animals by Kotake (2) in 1931. This reaction was studied in vitro by Mason and Berg (3, 4), who observed that slices and homogenates of rat liver converted both tryptophan and kynurenine to kynurenic acid. Similar preparations from rat kidney did not convert tryptophan to kynurenine or kynurenic acid, but had a somewhat great...
متن کاملKynurenine transaminase of rat kidney; a study of coenzyme dissociation.
Cell-free extracts of rat kidney catalyze the conversion of kynurenine to kynurenic acid by means of a transamination reaction (2). Such extracts lose kynurenine transaminase activity rapidly when added to phosphate buffer solutions with pH below 7 unless ol-ketoglutarate is added (2). Further studies in this laboratory have shown that this inactivation is completely reversed by the addition of...
متن کاملSubcellular distribution and properties of kynurenine transaminase in rat liver.
Kynurenine transaminase activity in rat liver was found in both the mitochondrial and supernatant fractions. The mitochondrial and supernatant fractions contained (a) kynurenine-pyruvate transaminase, which showed a preference for pyruvate as amino acceptor and a pH optimum between 8.0 and 8.5, and (b) kynurenine-alpha-oxoglutarate transaminase, with a preference for alpha-oxoglutarate and a pH...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1956
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65181-6