scholarly journals Ureotelism is inducible in the neotropical freshwater Hoplias malabaricus (Teleostei, Erythrinidae)

2004 ◽  
Vol 64 (2) ◽  
pp. 265-271 ◽  
Author(s):  
G. Moraes ◽  
V. L. P. Polez
Keyword(s):  
Specific Activity ◽  
Excretion Rate ◽  
Nitrogen Excretion ◽  
Urea Synthesis ◽  
Plasma Ammonia ◽  
Alkaline Water ◽  
Hoplias Malabaricus ◽  
Urea Excretion ◽  
Ammonia Transport ◽  
In The Wild

Increased environmental pH decreases ammonia transport through the gills, impairing nitrogenous waste. The consequent toxicity is usually drastic to most fishes. A few species are able to synthesize urea as a way to detoxify plasma ammonia. We studied three teleosts of the family Erythrinidae living in distinct environments, and assumed the biochemical behaviors would be different in spite of their being closely related species. Adult fish collected in the wild were submitted to alkaline water and the urea excretion rate was determined. The specific activity of urea cycle enzymes was determined in liver samples of fish from neutral waters. The studied species Hoplias lacerdae, Hoplerithrynus unitaeniatus, and Hoplias malabaricus are ureogenic. Urea synthesis is not a metabolic way to detoxify ammonia in H. lacerdae and Hoplerithrynus unitaeniatus exposed to an alkaline environment. The plasma ammonia profile of both species showed two distinct biochemical responses. Urea excretion of H. malabaricus was high in alkaline water, and the transition to ureotelism is proposed. The nitrogen excretion rate of H. malabaricus was among the highest values reported and the high urea excretion leads us to include this species as ureotelic in alkaline water.

Daily Pattern of Nitrogen Excretion and Oxygen Consumption of Sockeye Salmon (Oncorhynchus nerka) under Controlled Conditions

1975 ◽  
Vol 32 (12) ◽  
pp. 2479-2486 ◽  
Author(s):  
J. R. Brett ◽  
C. A. Zala
Keyword(s):  
Oxygen Consumption ◽  
Sockeye Salmon ◽  
Excretion Rate ◽  
Oncorhynchus Nerka ◽  
Ammonia Excretion ◽  
Nitrogen Excretion ◽  
Average Weight ◽  
Urea Excretion ◽  
Maintenance Ration ◽  
Exogenous Nitrogen

Measurements of the rate of ammonia and urea excretion of fingerling sockeye salmon (Oncorhynchus nerka) in fresh water were made at 2–3-hourly intervals throughout the day (average weight = 29 g; temperature = 15 C). One group of fish was fed a maintenance ration while another group was starved for 22 days. Ammonia excretion rose to a sharp peak of 35 mg N/kg per hour, 4–41/2 h after the start of feeding (at 0830) and fell to a baseline level of 8.2 mg N/kg per hour between 0200 and 0800. Urea excretion remained relatively steady at a mean rate of 2.2 mg N/kg per hour throughout the day, showing no diurnal response to feeding. Starved fish showed a nitrogen excretion rate close to that for both the steady state of urea excretion and the baseline rate of ammonia excretion of the fed fish. Oxygen consumption rose to a peak of 370 mg O2/kg per hour just before and during a 1-h feeding period, decreasing thereafter to a low of 170 mg O2/kg per hour at 0300 h. For the starved fish this diurnal metabolic fluctuation continued from the start in a variable and diminishing form whereas nitrogen excretion showed no such response. The results are discussed in relation to hatchery observations. We conclude that for nonstressed salmon at 15 C ammonia is the chief excretory product of exogenous nitrogen metabolism.

Subcellular localization and biochemical properties of the enzymes of carbamoyl phosphate and urea synthesis in the batrachoidid fishes Opsanus beta, Opsanus tau and Porichthys notatus

1995 ◽  
Vol 198 (3) ◽  
pp. 755-766 ◽  
Author(s):  
P Walsh
Keyword(s):  
Glutamine Synthetase ◽  
Subcellular Localization ◽  
Biochemical Properties ◽  
Nitrogen Excretion ◽  
Urea Synthesis ◽  
Carbamoyl Phosphate ◽  
Opsanus Beta ◽  
Opsanus Tau ◽  
Porichthys Notatus ◽  
The Family

The subcellular localization and biochemical properties of the enzymes of carbamoyl phosphate and urea synthesis were examined in three representatives of fishes of the family Batrachoididae, the gulf toadfish (Opsanus beta), the oyster toadfish (Opsanus tau) and the plainfin midshipman (Porichthys notatus). The primary objective of the study was to compare the biochemical characteristics of these fishes, which represent a range between ammoniotelism and ureotelism (O. beta being facultatively ureotelic), with previous patterns observed for an ammoniotelic teleost (Micropterus salmoides, the largemouth bass) and an obligate ureogenic elasmobranch (Squalus acanthias, the dogfish shark). The present study documents the expression of mitochondrial carbamoyl phosphate synthetase (CPSase) III and cytosolic CPSase II (and its associated enzymes of pyrimidine synthesis, dihydro-orotase and aspartate carbamoyltransferase) in the livers of all three batrachoidid species. Both mitochondrial and cytosolic activities of arginase were present in the livers of all three species, as were cytosolic glutamine synthetase and argininosuccinate synthetase and lyase. However, O. beta also showed mitochondrial glutamine synthetase activity and higher total hepatic levels of glutamine synthetase than either O. tau or P. notatus. Taken together, these observations confirm that the arrangement of these enzymes in the batrachoidid fishes has greater similarity to that of M. salmoides than to that of S. acanthias. However, differences within the family appear to coincide with the different nitrogen excretion strategies. O. tau and P. notatus are primarily ammoniotelic and most closely resemble the ammoniotelic M. salmoides, whereas ureotelism in O. beta is correlated with the presence of a mitochondrial glutamine synthetase and the ability to induce higher total glutamine synthetase activities than O. tau or P. notatus. Additionally, isolated mitochondria from O. beta were able to generate citrulline from glutamine, whereas those from O. tau were not. Also in contrast to S. acanthias, glutamine synthetase activities in the mitochondria of O. beta are consistently lower than those of CPSase III. This and other kinetic observations lend support to the hypothesis that glutamine synthetase may be an important regulatory control point in determining rates of ureogenesis in O. beta.

Urea Excretion in the Camel

1957 ◽  
Vol 188 (3) ◽  
pp. 477-484 ◽  
Author(s):  
Bodil Schmidt-Nielsen ◽  
Knut Schmidt-Nielsen ◽  
T. R. Houpt ◽  
S. A. Jarnum
Keyword(s):  
Glomerular Filtration Rate ◽  
Glomerular Filtration ◽  
Filtration Rate ◽  
Urea Concentration ◽  
Nitrogen Excretion ◽  
Renal Tubules ◽  
Urea Clearance ◽  
Plasma Urea ◽  
Urea Excretion ◽  
Plasma Urea Concentration

The nitrogen excretion was studied in the one-humped camel, Camelus dromedarius. When a growing camel was maintained on a low N intake (dates and hay) the amount of N excreted in the form of urea, NH3 and creatinine decreased to 2–3 gm/day. This decrease was caused by a drop in urea excretion from 13 gm to 0.2–0.5 gm/day. Urea given intravenously during low N intake was not excreted but was retained. (The camel like other ruminants can utilize urea for microbial synthesis of protein.) The renal mechanism for urea excretion was investigated by measuring urea clearance and glomerular filtration rate during a period of 7 months. During normal N intake about 40% of the urea filtered in the glomeruli were excreted in the urine while during low N intake only 1–2% were excreted. The variations in urea clearance were independent of the plasma urea concentration and of glomerular filtration rate, but were related to N intake and rate of growth. No evidence of active tubular reabsorption of urea was found since the urine urea concentration at all times remained higher than the simultaneous plasma urea concentration. The findings are not in agreement with the current concept for the mechanism of urea excretion in mammals. It is concluded that the renal tubules must either vary their permeability to urea in a highly selective manner or secrete urea actively.

scholarly journals Widespread use of emersion and cutaneous ammonia excretion in Aplocheiloid killifishes

2018 ◽  
Vol 285 (1884) ◽  
pp. 20181496 ◽  
Author(s):  
Michael D. Livingston ◽  
Vikram V. Bhargav ◽  
Andy J. Turko ◽  
Jonathan M. Wilson ◽  
Patricia A. Wright
Keyword(s):  
Ammonia Excretion ◽  
Nitrogen Excretion ◽  
Gaseous Ammonia ◽  
Urea Synthesis ◽  
Air Exposure ◽  
Ammonia Accumulation ◽  
Common Strategy ◽  
Kryptolebias Marmoratus ◽  
Amphibious Fishes ◽  
New Strategies

The invasion of land required amphibious fishes to evolve new strategies to avoid toxic ammonia accumulation in the absence of water flow over the gills. We investigated amphibious behaviour and nitrogen excretion strategies in six phylogenetically diverse Aplocheiloid killifishes ( Anablepsoides hartii, Cynodonichthys hildebrandi, Rivulus cylindraceus , Kryptolebias marmoratus, Fundulopanchax gardneri , and Aplocheilus lineatus ) in order to determine if a common strategy evolved . All species voluntarily emersed (left water) over several days, and also in response to environmental stressors (low O 2 , high temperature). All species were ammoniotelic in water and released gaseous ammonia (NH 3 volatilization) during air exposure as the primary route for nitrogen excretion. Metabolic depression, urea synthesis, and/or ammonia accumulation during air exposure were not common strategies used by these species. Immunostaining revealed the presence of ammonia-transporting Rhesus proteins (Rhcg1 and Rhcg2) in the skin of all six species, indicating a shared mechanism for ammonia volatilization. We also found Rhcg in the skin of several other fully aquatic fishes, implying that cutaneous ammonia excretion is not exclusive to amphibious fishes. Overall, our results demonstrate that similar nitrogen excretion strategies while out of water were used by all killifish species tested; possibly the result of shared ancestral amphibious traits, phenotypic convergence, or a combination of both.

Amino acid acylation: a mechanism of nitrogen excretion in inborn errors of urea synthesis

Science ◽  
1980 ◽  
Vol 207 (4431) ◽  
pp. 659-661 ◽  
Author(s):  
S Brusilow ◽  
J Tinker ◽  
M. Batshaw
Keyword(s):  
Amino Acid ◽  
Nitrogen Excretion ◽  
Urea Synthesis ◽  
Inborn Errors

Effect of glutamine on leucine metabolism in humans

1996 ◽  
Vol 271 (4) ◽  
pp. E748-E754 ◽  
Author(s):  
R. G. Hankard ◽  
M. W. Haymond ◽  
D. Darmaun
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Specific Activity ◽  
Excretion Rate ◽  
The Other ◽  
Anabolic Effect ◽  
Protein Breakdown ◽  
Glutamine Concentration ◽  
Putative Protein

The aim of this study was to determine whether the putative protein anabolic effect of glutamine 1) is mediated by increased protein synthesis or decreased protein breakdown and 2) is specific to glutamine. Seven healthy adults were administered 5-h intravenous infusions of L-[1-14C]leucine in the postabsorptive state while receiving in a randomized order an enteral infusion of saline on one day or L-glutamine (800 mumol.kg-1.h-1, equivalent to 0.11 g N/kg) on the other day. Seven additional subjects were studied using the same protocol except they received isonitrogenous infusion of glycine. The rates of leucine appearance (RaLeu), an index of protein degradation, leucine oxidation (OxLeu), and nonoxidative leucine disposal (NOLD), an index of protein synthesis, were measured using the 14C specific activity of plasma alpha-ketoisocaproate and the excretion rate of 14CO2 in breath. During glutamine infusion, plasma glutamine concentration doubled (673 +/- 66 vs. 1,184 +/- 37 microM, P < 0.05), whereas RaLeu did not change (122 +/- 9 vs. 122 +/- 7 mumol. kg-1.h-1), OxLeu decreased (19 +/- 2 vs. 11 +/- 1 mumol.kg-1.h-1, P < 0.01), and NOLD increased (103 +/- 8 vs. 111 +/- 6 mumol. kg-1.h-1, P < 0.01). During glycine infusion, plasma glycine increased 14-fold (268 +/- 62 vs. 3,806 +/- 546 microM, P < 0.01), but, in contrast to glutamine, RaLeu (124 +/- 6 vs. 110 +/- 4 mumol. kg-1.h-1, P = 0.02), OxLeu (17 +/- 1 vs. 14 +/- 1 mumol.kg-1.h-1, P = 0.03), and NOLD (106 +/- 5 vs. 96 +/- 3 mumol.kg-1.h-1, P < 0.05) all decreased. We conclude that glutamine enteral infusion may exert its protein anabolic effect by increasing protein synthesis, whereas an isonitrogenous amount of glycine merely decreases protein turnover with only a small anabolic effect resulting from a greater decrease in proteolysis than protein synthesis.

scholarly journals Overproduction of l-Lysine from Methanol by Methylobacillus glycogenes Derivatives Carrying a Plasmid with a Mutated dapA Gene

2001 ◽  
Vol 67 (7) ◽  
pp. 3064-3070 ◽  
Author(s):  
Hiroaki Motoyama ◽  
Hiroshi Yano ◽  
Yoko Terasaki ◽  
Hideharu Anazawa
Keyword(s):  
Amino Acid ◽  
Specific Activity ◽  
Test Tube ◽  
Amino Acid Sequences ◽  
Nutritional Requirement ◽  
Wild Type ◽  
Gene Encoding ◽  
Lysine Production ◽  
Obligate Methylotroph ◽  
In The Wild

ABSTRACT The dapA gene, encoding dihydrodipicolinate synthase (DDPS) partially desensitized to inhibition by l-lysine, was cloned from an l-threonine- andl-lysine-coproducing mutant of the obligate methylotrophMethylobacillus glycogenes DHL122 by complementation of the nutritional requirement of an Escherichia coli dapAmutant. Introduction of the dapA gene into DHL122 and AL119, which is the parent of DHL122 and an l-threonine producing mutant, elevated the specific activity of DDPS 20-fold andl-lysine production 2- to 3-fold with concomitant reduction of l-threonine in test tube cultures. AL119 containing thedapA gene produced 8 g of l-lysine per liter in a 5-liter jar fermentor from methanol as a substrate. Analysis of the nucleotide sequence of the dapA gene shows that it encodes a peptide with an M r of 30,664 and that the encoded amino acid sequence is extensively homologous to those of other organisms. In order to study the mutation that occurred in DHL122, the dapA genes of the wild type and AL119 were cloned and sequenced. Comparison of the nucleotide sequences of the dapA genes revealed that the amino acid at residue 88 was F in DHL122 whereas it was L in the wild type and AL119, suggesting that this amino acid alteration that occurred in DHL122 caused the partial desensitization of DDPS to the inhibition byl-lysine. The similarity in the amino acid sequences of DDPS in M. glycogenes and other organisms suggests that the mutation of the dapA gene in DHL122 is located in the region concerned with interaction of the allosteric effector,l-lysine.

scholarly journals Purification and properties of uroporphyrinogen III synthase (co-synthase) from an overproducing recombinant strain of Escherichia coli K-12

1989 ◽  
Vol 264 (2) ◽  
pp. 397-402 ◽  
Author(s):  
A F Alwan ◽  
B I A Mgbeje ◽  
P M Jordan
Keyword(s):  
Escherichia Coli ◽  
Specific Activity ◽  
Heat Inactivation ◽  
Gene Encoding ◽  
Ph Optimum ◽  
Nitrobenzoic Acid ◽  
Purification And Properties ◽  
Lower Reactivity ◽  
In The Wild ◽  
K 12

The Escherichia coli hemD gene, encoding the enzyme uroporphyrinogen III synthase (co-synthase), was cloned into multi-copy plasmids in E. coli cells that were used to generate strains producing up to 1000 times the concentration of the synthase in the wild-type. The enzyme was purified to homogeneity from these strains in milligram amounts. The enzyme is a monomer of Mr 28,000 with an isoelectric point of 5.2 and a pH optimum of 7.8. The specific activity of the purified synthase is 1500 units/mg and the Km for the substrate, pre-uroporphyrinogen, is 5 microM. The N-terminal sequence of the enzyme is Ser-Ile-Leu-Val-Thr-Arg-Pro-Ser-Pro-Ala-Gly-, in agreement with the gene-derived protein sequence. The enzyme contains four 5,5′-dithiobis-(2-nitrobenzoic acid)-titratable groups, one reacting rapidly with the reagent and three further groups having lower reactivity. The enzyme is heat-sensitive, and during heat inactivation all four thiol groups become equally available for reaction.

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