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The purpose of the present study was to investigate erythrocyte membrane abnormalities in hypertension by means of an electron spin resonance and spin-label technique. The erythrocytes from spontaneously hypertensive rats (SHR) and humans with untreated essential hypertension were examined and compared with their normotensive counterparts, and electron spin(More)
Kynurenine-pyruvate aminotransferase (KPT), the enzyme responsible for the biosynthesis of the endogenous excitatory amino acid receptor antagonist kynurenic acid, was purified to homogeneity from rat kidney, as judged by polyacrylamide and sodium dodecyl sulfate electrophoresis. The protein appeared to consist of 2 identical subunits of approximately 48(More)
The effect of caffeic acid on hydroxyl radical formation through a reaction, which contained 0.22 M carbonate buffer (pH 7.4), 0.22 mM 3-hydroxyanthranilic acid, 87 mM 5,5-dimethyl-1-pyrroline-N-oxide (DMPO), 2.9 mM hydrogen peroxide, and 14 microM FeCl3, was investigated. The addition of 30 microM caffeic acid resulted in the decrease of hydroxyl radical(More)
Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase was characterized, taking advantage of its induction by bacterial lipopolysaccharide. Our results demonstrated that in various tissues, N-formylkynurenine produced by the dioxygenase from tryptophan was rapidly hydrolyzed into kynurenine by a kynurenine formamidase, but it was not(More)
Two major 2-aminoadipate aminotransferase (AadAT) activities of human liver extract were separated by DEAE-Sepharose column chromatography. The faster eluting enzyme was designated AadAT-I and the other one AadAT-II. AadAT-I had a hgih Km value for aminoadipate, 20 mmol/l, and a low Km value for glutamate, 1.4 mmol/l. In contrast, AadAT-II had a low Km(More)
Mitochondrial extracts of dog, cat, rat and mouse liver contain two forms of alanine-glyoxylate aminotransferase (EC 2.6.1.44): one, designated isoenzyme 1, has mol.wt. approx. 80 000 and predominates in dog and cat liver; the other, designated isoenzyme 2, has mol.wt. approx. 175 000 and predominates in rat and mouse liver. In rat and mouse liver,(More)
The organ distribution of rat histidine-pyruvate aminotransferase isoenzymes 1 and 2 was examined by using an isoelectric-focusing technique. Isoenzyme 1 (pI8.0) is present only in the liver and its activity is increased by the injection of glucagon, whereas isoenzyme 2 (pI5.2) is distributed in all tissues (liver, kidney, brain and heart) tested, and is(More)
Induction by interferon-gamma of indoleamine 2,3-dioxygenase (a tryptophan degradation enzyme) was examined with 11 human cell lines. The enzyme induction was demonstrated in 7 of the 11 cell lines. The induced enzyme in each of the 7 cell lines was identical to the enzyme purified from human placenta, as evidenced by immunoblot analysis with a monoclonal(More)