Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “AMMONIA”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources
PubMed1992

Fiber-optic ammonia sensor for measuring synaptic glutamate and extracellular ammonia.

A fiber-optic ammonia gas sensor designed for neurochemical applications is presented. Parameters evaluated in terms of effect on the steady-state and dynamic response of this sensor include the indicator dye, concentrations of indicator and total ammonia nitrogen in the internal solution, volume of the internal solution, structure of the gas-permeable membrane, and temperature. The final ammonia sensor responds over the concentration range from 7 to 3000 nM with a limit of detection of 7 nM and response times ranging from 2 to 5 min. Glutamate oxidase is immobilized at the tip of this ammonia sensor to provide a glutamate biosensor with a detection limit of 0.1 microM when operated at pH 7.8. In addition, this ammonia sensor is used to measure extracellular ammonia levels in perfused retinal and eye-cup tissue preparations. These measurements indicate a calcium-dependent, potassium-evoked release of ammonia during these depolarization conditions.

Ammonia↗
PubMed2000

An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia.

The heterodimeric carbamoyl phosphate synthetase (CPS) from Escherichia coli catalyzes the formation of carbamoyl phosphate from bicarbonate, glutamine, and two molecules of ATP. The enzyme catalyzes the hydrolysis of glutamine within the small amidotransferase subunit and then transfers ammonia to the two active sites within the large subunit. These three active sites are connected via an intermolecular tunnel, which has been located within the X-ray crystal structure of CPS from E. coli. It has been proposed that the ammonia intermediate diffuses through this molecular tunnel from the binding site for glutamine within the small subunit to the phosphorylation site for bicarbonate within the large subunit. To provide experimental support for the functional significance of this molecular tunnel, residues that define the interior walls of the "ammonia tunnel" within the small subunit were targeted for site-directed mutagenesis. These structural modifications were intended to either block or impede the passage of ammonia toward the large subunit. Two mutant proteins (G359Y and G359F) display kinetic properties consistent with a constriction or blockage of the ammonia tunnel. With both mutants, the glutaminase and bicarbonate-dependent ATPase reactions have become uncoupled from one another. However, these mutant enzymes are fully functional when external ammonia is utilized as the nitrogen source but are unable to use glutamine for the synthesis of carbamoyl-P. These results suggest the existence of an alternate route to the bicarbonate phosphorylation site when ammonia is provided as an external nitrogen source.

Alanine↗
PubMed1992

Transbranchial ammonia gradients and acid-base responses to high external ammonia concentration in rainbow trout (Oncorhynchus mykiss) acclimated to different salinities.

Transbranchial ammonia gradients and blood acid-base status have been examined in rainbow trout acclimated to fresh water (FW), 33% sea water (33% SW) and sea water (SW) and exposed to 1.0 mmol l-1 total ammonia (TAmm) at pH 7.9 for 24 h. At all three salinities trout maintained large negative (inwardly directed) NH3 and NH4+ gradients throughout the exposure, presumably by active excretion of NH4+ to counteract the passive inward diffusion of ammonia. Analysis of blood non-respiratory acid-base status (delta H+m) revealed an acid load in FW trout and a base load in SW trout following 24 h of exposure. This indicates that active NH4+/H+ exchange predominates in FW whereas NH4+/Na+ is the principal exchange utilised in SW under these experimental conditions. The plasma TAmm load incurred during ammonia exposure increased with salinity. Compared to FW trout, plasma TAmm values were 34 and 73% higher in the 33% SW and SW trout, respectively, after 24 h. This cannot be explained by differences in the prevailing transbranchial PNH3 gradient because ambient PNH3 was substantially lower at the higher salinities (due to higher pK' and solubility values). We interpret the difference between FW and SW trout as an increased permeability to NH4+ in fish acclimated to the higher-salinity environments. Transbranchial diffusion of NH4+ is, therefore, probably more important as a route for ammonia excretion in SW than in FW trout, especially considering the favourable transepithelial potentials normally found in SW teleosts. In addition, increased NH4+ permeability implies that the toxicity of ammonia will be greater in seawater than in freshwater teleosts and should not simply be measured as a function of the unionised ammonia concentration when considering seawater-adapted species.

Acclimatization↗
PubMed2001

Ammonia detoxification and localization of urea cycle enzyme activity in embryos of the rainbow trout (Oncorhynchus mykiss) in relation to early tolerance to high environmental ammonia levels.

The present study investigated the role of ammonia as a trigger for hatching, mechanisms of ammonia detoxification and the localization of urea cycle enzymes in the early life stages of freshwater rainbow trout (Oncorhynchus mykiss). The key urea cycle enzyme carbamoyl phosphate synthetase III was found exclusively in the embryonic body (non-hepatic tissues); related enzymes were distributed between the liver and embryonic body. 'Eyed-up' trout embryos were exposed either acutely (2h) to 10 mmol l(-1) NH(4)Cl or chronically (4 days) to 0.2 mmol l(-1) NH(4)Cl. Time to hatching was not affected by either acute or chronic NH(4)Cl exposure. Urea levels, but not ammonia levels in the embryonic tissues, were significantly higher than in controls after both acute and chronic NH(4)Cl exposure, whereas there were no significant changes in urea cycle enzyme activities. Total amino acid levels in the embryonic tissues were unaltered by chronic ammonia exposure, but levels of most individual amino acids and total amino acid levels in the yolk were significantly lower (by 34-58%) than in non-exposed controls. The data indicate that trout embryos have an efficient system to prevent ammonia accumulation in embryonic tissue, by conversion of ammonia to urea in embryonic tissues and through elevation of ammonia levels in the yolk.

Ammonia↗
PubMed1982

The measurement of erythrocyte ammonia using the Hyland Ammonia kit.

We modified the Hyland Ammonia kit for plasma to measure blood ammonia from which the erythrocyte ammonia is calculated. Our modified method gave good recoveries and its precision based on replicate assays was excellent (CV less than 3.0%). The within-day and day-to-day precision was determined from pooled blood and aqueous ammonia solution respectively. The precision calculated from duplicate results was not as good but agreed with other published values. A critical examination of Hyland's method showed the efficiency of resin adsorption to be 78%, and that the resin caused a 16% reduction in the Berthelot reaction, while 4 mol/l NaCl increased the reaction by about 11%. Blood specimens for ammonia can be frozen but specimen instability occurred during the thawing process. Measurement of ammonia directly on frozen specimens overcomes this problem. The reference range for erythrocyte ammonia was 14.5-46.1 (mean 30.1, SD 7.9) mumol/l.

Adsorption↗
PubMed2003

Distinct thermodynamics for the formation and cleavage of N-H bonds in aniline and ammonia. Directly-observed reductive elimination of ammonia from an isolated amido hydride complex.

The reactions of aryl and alkylamines with the (PCP)Ir fragment (PCP = 1,3-di-tert-butylphosphinobenzene) were studied to determine the reactivities and stabilities of amine and amido hydride complexes relative to C-H activation products. Reaction of aniline with the (PCP)Ir unit generated from (PCP)IrH2 and norbornene resulted in the N-H oxidative addition product (PhNH)(H)Ir(PCP) (1a). In contrast, reaction of this fragment with ammonia gave the ammonia complex (NH3)Ir(PCP) (2). The amido hydride complex that would be formed by oxidative addition of ammonia, (PCP)Ir(NH2)(H) (1b), was generated independently by deprotonation of the ammonia complex (NH3)Ir(H)(Cl)(PCP) (3) with KN(SiMe3)2 at low temperature. This amido hydride complex underwent reductive elimination at room temperature to form the ammonia complex 2. Addition of CO to anilide complex 1a gave (PCP)Ir(PhNH)(H)(CO) (4a). Addition of CNtBu to terminal amido complex 1b formed (PCP)Ir(NH2)(H)(CNtBu) (4b), the first structurally characterized iridium amido hydride. Complexes 4a and 4b underwent reductive elimination of aniline and ammonia; parent amido complex 4b reacted faster than anilide 4a. These observations suggest distinct thermodynamics for the formation and cleavage of N-H bonds in aniline and ammonia. Complexes 1a, 2, 4a, and 4b were characterized by single-crystal X-ray diffraction methods.

Journal Article↗
PubMed1994

EFFECTS OF AMMONIA LOADING ON PORCELLIO SCABER: GLUTAMINE AND GLUTAMATE SYNTHESIS, AMMONIA EXCRETION AND TOXICITY

The effects of ammonia loading in the terrestrial isopod Porcellio scaber were studied by exposing animals to atmospheres of high PNH3. Isopods show a remarkable tolerance of elevated ambient PNH3, with an LD50 of 89 Pa for a 7-day exposure. However, haemolymph total ammonia concentrations generally remained below 5 mmol l-1 (PNH3=0.37 Pa) over the range of ambient ammonia levels used (6.6­165 Pa). Following a 7-day loading period, whole-animal glutamine (Gln) and glutamate (Glu) levels increased in direct proportion to ambient PNH3, reaching values of 35 µmol g-1 fresh mass for glutamine and 12 µmol g-1 fresh mass for glutamate in 99 Pa PNH3; these correspond to control levels of 7.5 µmol g-1 fresh mass and 5.9 µmol g-1 fresh mass, respectively. Following transfer to ammonia-free chambers, NH3 excretion rates were augmented five- to sixfold relative to non-loaded controls. Ammonia volatilization subsequently declined, approaching control levels after 8­9 days. Levels of Gln and Glu showed a concomitant decline to 13.7 µmol g-1 fresh mass and 9.2 µmol g-1 fresh mass, respectively. The results suggest that these amino acids function in ammonia sequestration and, hence, detoxification. Calculations indicate that mobilization of amino groups by deamination of accumulated Gln and Glu could explain 35 % of the increased ammonia production. Implications of NH3 volatilization for acid­base balance are discussed.

Journal Article↗
PubMed1989

Studies of ammonia loading: effects of rate of delivery and enhanced removal of NH4 on blood levels of ammonia and coma induction.

Using dose-response curves, the dose of NH4Ac inducing coma in one-half of the animals was increased by 60 to 80% after 1 mmol of arginine. The larger increase occurred in larger rats but was not proportional to the increase in weight. Incremental subcoma doses of NH4 raised the amount of NH4 required for inducing coma and the brain level of ammonia at the point of coma. After a portacaval shunt the results were similar, although lower doses of NH4 were required from the beginning. Blood ammonias after a loading dose (1.25 mmol) of NH4 were influenced by the duration of a preinfusion of NH4 and by the preinjection of various amino acids involved in the disposal of NH4 in the urea cycle. The amount of reduction in blood ammonia by ornithine and arginine compounds was less the longer the preinfusion of NH4. Blood ammonia was not lowered by glutamate at any time but was increased with longer preinfusion periods. Hepatectomy (Hx) reduced the removal of an NH4 load. After a modest load (0.85 mmol) of NH4, blood ammonia increased 5-fold, over that of sham-operated rats, with 70% Hx and 15-fold with 90% Hx. Ornithine reduced these blood ammonias by about 50%. Arginine had no effect. These studies indicate ways of reducing toxicity of NH4 and factors that predispose to or enhance toxicity.

Amino Acids↗
PubMed2003

Role of ureogenesis in tackling problems of ammonia toxicity during exposure to higher ambient ammonia in the air-breathing walking catfish Clarias batrachus.

In the present study, the possible role of ureogenesis to avoid the accumulation of toxic ammonia to a lethal level under hyper-ammonia stress was tested in the air-breathing walking catfish Clarias batrachus by exposing the fish at 25 mM NH4Cl for 7 days. Excretion of ammonia by the NH4Cl-exposed fish was totally suppressed, which was accompanied by significant accumulation of ammonia in different body tissues. The walking catfish, which is otherwise predominantly ammoniotelic, turned totally towards ureotelism from ammoniotelism with a 5- to 6-fold increase of urea-N excretion during exposure to higher ambient ammonia. Stimulation of ureogenesis was accompanied with significant increase of some of the key urea cycle enzymes such as carbamyl phosphate synthetase (urea cycle-related), argininosuccinate synthetase and argininosuccinate lyase both in hepatic and non-hepatic tissues. Due to this unique physiological strategy of turning towards ureotelism from ammoniotelism via the induced urea cycle, this air-breathing catfish is able to survive in very high ambient ammonia, which they face in certain seasons of the year in the natural habitat.

Air↗
PubMed2006

Ammonia removal from livestock wastewater by ammonia-assimilating microorganisms immobilized in polyvinyl alcohol.

We isolated ammonia-assimilating microorganisms from the livestock manure treatment systems and evaluated their ammonia-assimilating ability. Many isolates utilized ammonia at high rates when they were purely cultivated in a nitrogen-limited medium to which sterilized lagoon extract had been added. Some isolates that were immobilized in polyvinyl alcohol (PVA) utilized ammonia present in the media containing viable lagoon microorganisms. Staining with 4',6'-diamidino-2-phenylindole (DAPI) indicated that the immobilized high ammonia-assimilating isolates grew dominantly within the PVA beads. High ammonia-assimilating isolates in the mixed culture containing viable lagoon microorganisms were identified as Pseudomonas spp. and member of Rhizobiaceae species by partial sequencing of the 16S ribosomal DNA.

Ammonia↗
PubMed1996

Arterial ammonia with Blood Ammonia Checker II and with indophenol reaction to assess presence of hepatic encephalopathy.

Hepatic encephalopathy (HE) is associated with elevated arterial ammonia levels. The relationship is variable, in part due to ammonia methodology. One method, based on the indophenol reaction (IPh), is interfered with a number of amino acids including all aromatic amino acids. We have determined arterial ammonia simultaneously with the Blood Ammonia Checker II (BAC) as reference method and with the IPh method. The difference BAC-IPh, mumol/l, was assumed to express the interference in the indophenol method (IFI) by amino acids. It may be positive or negative. The aim was to establish the value of BAC in comparison with IPh in the diagnosis of liver disease and overt HE and to assess any added value of IFI. Of two reference groups without disturbances, A (n = 39) had not and B (n = 13) had encephalopathy. Group C consisted of 125 liver patients (34 no cirrhosis, 91 cirrhosis) of which 55 had no manifest HE (C:HE-) and 70 had HE (C:HE+). Median BAC ammonia nitrogen (NH3-N), mumol/l: A 21, B 35, C 80, C:HE - 57 and C:HE+ 98 (A < B < C and A < B < C:HE - < C:HE +, P < 0.001). Median IPh NH3-N, mumol/l: A 27, B 30, C 30, C:HE - 25 and C:HE + 35 mumol/l (A = B = C and C:HE - < C:HE+, P < 0.01). IFI medians: A -6, B 3, C 40, C:HE - 29 and C:HE + 58 mumol/l (A < B (P < 0.05) < C (P < 0.0001); A, B < C:HE - and C:HE+; C:HE- < C:HE + (all P < 0.0001)). While BAC correlated weakly with IPh in the (sub)groups C, C:HE-, C:HE+ (r = 0.3, 0.3, 0.4, P < 0.05), it correlated strongly with IFI (r = 0.9, 0.9, 0.8, P < 0.0001). There was no correlation between IPh and IFI. BAC, as well as IFI, could discriminate all liver patients (C) from both reference groups A and B with 100% positive likelihoods. BAC, IPh and IFI could discriminate between HE- and HE+. To differentiate cirrhosis from non-cirrhosis the specificity of IPh was uniformly high and the sensitivity satisfactory, whereas BAC had a high sensitivity but an insufficient specificity. In conclusion, in blood, BAC is the ammonia determination of choice. It differentiates between reference groups (encephalopathic or not) and liver disease and the more so HE. The combination of BAC and IPh (indicating IFI) may eventually be shown useful to rapidly assess the severity of underlying liver disease in HE patients. In other biological fluids, IPh is excellent when the inhibiting influence of non-protein nitrogen substances is absent or can be eliminated.

Adult↗
PubMed1986

Time course of urinary excretion of intraportal ammonia as uric acid and ammonia in chickens fed low- or high-protein diet.

15N-ammonia was intraportally infused for 6 hr into chickens fed 5% or 20% protein diet to examine the time course of urinary excretion of intraportal ammonia and dietary effects on it. Urinary ammonia increased linearly for the first hour to the same extent in both dietary groups and thereafter further in the low-protein group. Urinary uric acid derived from the intraportal ammonia adaptively increased and reached a steady state level within 1.5 hr. This level was four times higher in the high-protein group. The infused ammonia was excreted into urine as both ammonia and uric acid, in relatively high proportions in the chickens fed the low-protein diet but was almost all excreted as uric acid in those fed the high-protein diet.

Ammonia↗
PubMed1976

Relationship between ruminal ammonia and nonprotein nitrogen utilization by ruminants. III. Influence of intraruminal urea infusion on ruminal ammonia concentration.

In three trials, we studied the effect of incremental amounts of intraruminally infused urea on mean ruminal ammonia concentration of steer fed at 2-h intervals. Basal rations contained these percentages of crude protein and total digestible nutrients (dry matter basis); Trial I, 11.1 and 81; Trial II, 6.0 and 54; Trial III, 6.5 and 58. Mean ruminal ammonia concentration reached 5 mg ammonia nitrogen/100 ml rumen fluid at crude protein equivalents of 12.0, 9.3, and 9.4% in I, II, and III. Once ruminal ammonia began to accumulate, there was a linear relationship between intake of urea and mean concentration of amino acids of plasma, serving as an indirect measure of amino acid absorption from the intestine, was not increased by increased intake of urea in III. Results of this experiment support the concept from in vitro data that microbial protein synthesis is unaffected by ruminal ammonia concentration in excess of 5 mg ammonia nitrogen/100 ml rumen fluid.

Amino Acids↗
PubMed2004

Genera-specific immunofluorescence labeling of ammonia oxidizers with polyclonal antibodies recognizing both subunits of the ammonia monooxygenase.

Polyclonal antibodies that recognize the two subunits AmoA and AmoB of the ammonia monooxygenase (AMO) were applied to identify ammonia-oxidizing bacteria by immunofluorescence (IF) labeling in pure, mixed, and enriched cultures. The antibodies against the AmoA were produced using a synthetic peptide of the AmoA of Nitrosomonas eutropha, whereas the antibodies against the AmoB had been developed previously is against the whole B-subunit of the AMO [Pinck et al. (2001) Appl Environ Microbiol 67:118-124]. Using IF labeling, the AmoA antibodies were specific for the detection of all species of the genus Nitrosomonas. In contrast, the antiserum against AmoB labeled all genera of ammonia oxidizers of the beta-subclass of Proteobacteria (Nitrosomonas, Nitrosospira, Nitrosolobus, and Nitrosovibrio). The fluorescence signals of the AmoA antibodies were spread all over the cells, whereas the signals of the AmoB antibodies were associated with the cytoplasmic membranes. The specificity of the reactions of the antisera with ammonia oxidizers were proven in pure and mixed cultures, and the characteristic IF labeling and the morphology of the cells enabled their identification at the genus level. The genus-specific IF labeling could be used to identify ammonia oxidizers enriched from various habitats. In enrichment cultures of natural sandstone, cells of the genera Nitrosomonas, Nitrosovibrio, and Nitrosospira were detected. Members of the genus Nitrosovibrio and Nitrosolobus were most prominent in enriched garden soil samples, whereas members of the genus Nitrosomonas dominated in enriched activated sludge. The antibodies caused only slight background fluorescence on sandstone and soil particles compared to oligonucleotide probes, which could not be used to detect ammonia oxidizers on these materials because of strong nonspecific fluorescence.

Antibodies, Bacterial↗
PubMed1993

Inhibition of Ammonia Oxidation in Nitrosomonas europaea by Sulfur Compounds: Thioethers Are Oxidized to Sulfoxides by Ammonia Monooxygenase.

Organic sulfur compounds are well-known nitrification inhibitors. The inhibitory effects of dimethylsulfide, dimethyldisulfide, and ethanethiol on ammonia oxidation by Nitrosomonas europaea were examined. Both dimethylsulfide and dimethyldisulfide were weak inhibitors of ammonia oxidation and exhibited inhibitory characteristics typical of substrates for ammonia monooxygenase (AMO). Depletion of dimethylsulfide required O(2) and was prevented with either acetylene or allylthiourea, two inhibitors of AMO. The inhibition of ammonia oxidation by dimethylsulfide was examined in detail. Cell suspensions incubated in the presence of ammonia oxidized dimethylsulfide to dimethyl sulfoxide. Depletion of six other thioethers was also prevented by treating cell suspensions with either allylthiourea or acetylene. The oxidative products of three thioethers were identified as the corresponding sulfoxides. The amount of sulfoxide formed accounted for a majority of the amount of sulfide depleted. By using gas chromatography coupled with mass spectrometry, allylmethylsulfide was shown to be oxidized to allylmethylsulfoxide by N. europaea with the incorporation of a single atom of O derived from O(2) into the sulfide. This result supported our conclusion that a monooxygenase was involved in the oxidation of allylmethylsulfide. The thioethers are concluded to be a new class of substrates for AMO. This is the first report of the oxidation of the sulfur atom by AMO in whole cells of N. europaea. The ability of N. europaea to oxidize dimethylsulfide is not unique among the ammonia-oxidizing bacteria. Nitrosococcus oceanus, a marine nitrifier, was also demonstrated to oxidize dimethylsulfide to dimethyl sulfoxide.

Journal Article↗
PubMedDate not supplied

Accumulation of ammonia and changes in the activity of some ammonia metabolizing enzymes during brain ischemia/reperfusion injury in rats.

The ammonia concentration and changes in the activity of ammonia metabolizing enzymes in the brain tissue during ischemia/reperfusion were investigated in rats. During ischemia (0.5 h) we found a statistically significant increase in brain ammonia concentration and a significant decrease in glutamate dehydrogenase activity. After 1 h of reperfusion, a further accumulation of ammonia concentration was observed. Furthermore, the brain glutamine syntethase and glutamate dehydrogenase were decreased, whereas the brain glutaminase activity was increased. The causes for the changed activities of some ammonia metabolizing enzymes in brain after ischemia/reperfusion have been discussed.

Ammonia↗
PubMed1985

Ammonia production by IMR-90 fibroblast cultures: effects of ammonia on glutathione, gamma-glutamyl transpeptidase, lysosomal enzymes, and cell division.

gamma-Glutamyl transpeptidase has multi-catalytic activities. It degrades glutathione and can produce ammonia from glutamine. The present study was designed to examine whether the decreased cell proliferation, cellular glutathione content and concurrent increase in ammonia production in senescent cells in culture are the result of increased gamma-glutamyl transpeptidase activity. We used IMR-90 fibroblast and 3T3 LI preadipocyte cultures. The cellular glutathione content depended upon cell proliferation and cell density. The glutathione content was higher in cells at logarithmic growth, and lower at stationary growth or post confluency; dead cells had no detectable glutathione by the method currently used. The glutathione content was minimal in "old" IMR-90 cells, regardless of cell density. On the other hand, an increase occurred in the unit number of molecules of bound 5-iodoacetoamidofluorescein, an active-site directed stoichiometric inhibitor of transpeptidase. That result corresponded favorably with the increased enzyme activity, suggesting that the number of enzyme molecules per cell was increased. The inhibition of ammonia production of the cultures by inhibition of gamma-glutamyl transpeptidase by 5-iodoacetoamidofluorescein and reversible inhibition of ammonia production by a serine-borate mixture were consistent with our postulate. Addition of NH4Cl (0.1 mM) to IMR-90 cultures caused increased activities of transpeptidase and some of the lysosomal enzymes; concurrently, the amount of cellular glutathione and the number of cell divisions decreased. This suggests that the increased ammonia production presumably resulting from glutaminase activity of the observed increase of transpeptidase may profoundly affect certain cellular functions.

Adipose Tissue↗
PubMed1980

A dynamic study of rectally absorbed ammonia in liver cirrhosis using [13N]ammonia and a positron camera.

[13N]Ammonia produced by the cyclotron was instilled intrarectally in patients with cirrhosis and other liver diseases to study the turnover of rectally absorbed [13N]ammonia. A positron camera connected to an on-line computer system was used for the measurement of sequential changes of 13N activity in blood and for coincidence positron imaging of the liver and heart. 13N activity over the head was also recorded. Chromatographic analysis of 13N-labeled substances in blood was carried out using a Dowex 50Wx8 column at varying times after the administration. In the control, [13N]ammonia was absorbed quickly and visualized the liver, whereas in patients with cirrhosis, the lungs and heart were first visualized, and 13N activity over the head was also higher. It was suggested that a large proportion of absorbed [13N]ammonia bypassed hepatocytes and reached peripheral tissues in cirrhosis. The heart/liver ratio of 13N and 13N over the head were correlated with various indices of portal hypertension. The relative proportion of nonammonia 13N metabolites in blood was lower at 5 and 15 min after administration in cirrhosis, suggesting a reduced capacity of the liver to remove and metabolize ammonia.

Acute Disease↗