Enzymological studies on glutamic acid metabolism in the liver (Report II) The relationship between glutamine synthetase, glutamic dehydrogenase and urea cycle enzymes in ammonia detoxication

1967 ◽  
Vol 2 (2) ◽  
pp. 132-132
Author(s):  
T. Miyake ◽  
K. Ito ◽  
T. Tamai ◽  
T. Tateyama
Keyword(s):  
Glutamine Synthetase ◽  
Glutamic Acid ◽  
Acid Metabolism ◽  
Urea Cycle ◽  
Glutamic Dehydrogenase ◽  
The Relationship ◽  
Urea Cycle Enzymes

scholarly journals The rate of adaptation of urea cycle enzymes, aminotransferases and glutamic dehydrogenase to changes in dietary protein intake

1974 ◽  
Vol 32 (2) ◽  
pp. 353-373 ◽  
Author(s):  
T. K. Das ◽  
J. C. Waterlow
Keyword(s):  
Enzyme Activity ◽  
Dietary Protein ◽  
Urea Cycle ◽  
Rate Of Change ◽  
Simple Relationship ◽  
Hepatic Enzymes ◽  
Common Control ◽  
Glutamic Dehydrogenase ◽  
Steady State Levels ◽  
Urea Cycle Enzymes

1. Measurements were made, at 6 h intervals, of urinary nitrogen output and of the activity of some hepatic enzymes in the rat during adaptation from one level of dietary protein to another. The enzymes measured were arginase (EC 3.5.3.1), argininosuccinate lyase (EC 4.3.2.1), argininosuccinate synthetase (EC 6.3.4.5), glutamate dehydrogenase (EC 1.4.1.2) and alanine and aspartate aminotransferases (EC 2.6.1.2 and EC 2.6.1.1).2. Completeness of urine collection, which was essential for these experiments, was checked by recovery of injected [131I]iodide.3. When the dietary protein content was reduced from 135 to 45 g casein/kg, the urinary N output and the activities of the hepatic enzymes reached their new steady-state levels in 30 h. The reverse adaptation, from 45 to 135 g casein/kg, was also complete in 30 h.4. The rate of change of enzyme activity and the final activity as percentage of initial activity were very similar for all six enzymes, suggesting a common control mechanism. The calculated half-lives of the enzymes were of the order of 7 h, which is very much shorter than those found by previous workers.5. There was no simple relationship between the activity of the urea cycle enzymes and the amount of N excreted. When an equal amount of gelatin was substituted for casein the N output was doubled but there was no change in the activity of the liver enzymes.6. The results suggest that the activity of the urea cycle enzymes depends in part on the amount of N available for excretion after the demands for synthesis have been met. The enzymes, however, appear to be present in excess so that an increased N load was not necessarily accompanied by an increase in enzyme activity.

Isoleucine Plays an Important Role for Maintaining Immune Function

2019 ◽  
Vol 20 (7) ◽  
pp. 644-651 ◽  
Author(s):  
Changsong Gu ◽  
Xiangbing Mao ◽  
Daiwen Chen ◽  
Bing Yu ◽  
Qing Yang
Keyword(s):  
Amino Acids ◽  
Acid Metabolism ◽  
Branched Chain Amino Acids ◽  
Whole Body ◽  
Immune Functions ◽  
Host Defense Peptides ◽  
Innate And Adaptive Immunity ◽  
Physiological Functions ◽  
Branched Chain ◽  
The Relationship

Branched chain amino acids are the essential nutrients for humans and many animals. As functional amino acids, they play important roles in physiological functions, including immune functions. Isoleucine, as one of the branched chain amino acids, is also critical in physiological functions of the whole body, such as growth, immunity, protein metabolism, fatty acid metabolism and glucose transportation. Isoleucine can improve the immune system, including immune organs, cells and reactive substances. Recent studies have also shown that isoleucine may induce the expression of host defense peptides (i.e., β-defensins) that can regulate host innate and adaptive immunity. In addition, isoleucine administration can restore the effect of some pathogens on the health of humans and animals via increasing the expression of β-defensins. Therefore, the present review will emphatically discuss the effect of isoleucine on immunity while summarizing the relationship between branched chain amino acids and immune functions.

scholarly journals Induction of urea cycle enzymes by glucagon and dexamethasone in monolayer cultures of adult rat hepatocytes.

1982 ◽  
Vol 257 (9) ◽  
pp. 5061-5067
Author(s):  
R C Lin ◽  
P J Snodgrass ◽  
D Rabier
Keyword(s):  
Urea Cycle ◽  
Rat Hepatocytes ◽  
Adult Rat ◽  
Monolayer Cultures ◽  
Adult Rat Hepatocytes ◽  
Urea Cycle Enzymes

scholarly journals Carnitine administration to juvenile visceral steatosis mice corrects the suppressed expression of urea cycle enzymes by normalizing their transcription.

1992 ◽  
Vol 267 (8) ◽  
pp. 5032-5035
Author(s):  
M Horiuchi ◽  
K Kobayashi ◽  
M Tomomura ◽  
M Kuwajima ◽  
Y Imamura ◽  
...  
Keyword(s):  
Urea Cycle ◽  
Urea Cycle Enzymes

Glutamic acid metabolism in vivo: The effects of pretreatment with morphine sulphate

1964 ◽  
Vol 13 (11) ◽  
pp. 1507-1511 ◽  
Author(s):  
Laurence S. Maynard ◽  
Victor J. Schenker
Keyword(s):  
Glutamic Acid ◽  
Acid Metabolism ◽  
Morphine Sulphate

scholarly journals Unfolding of Helical Poly(L-Glutamic Acid) in N,N-Dimethylformamide Probed by Pyrene Excimer Fluorescence (PEF)

Polymers ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 1690
Author(s):  
Weize Yuan ◽  
Remi Casier ◽  
Jean Duhamel
Keyword(s):  
Glutamic Acid ◽  
Local Density ◽  
Guanidine Hydrochloride ◽  
Racemic Mixture ◽  
Excimer Fluorescence ◽  
Excimer Formation ◽  
Blob Model ◽  
Α Helix ◽  
The Relationship ◽  
Pyrene Excimer Formation

The denaturation undergone by α–helical poly(L-glutamic acid) (PLGA) in N,N-dimethylformamide upon addition of guanidine hydrochloride (GdHCl) was characterized by comparing the fluorescence of a series of PLGA constructs randomly labeled with the dye pyrene (Py-PLGA) to that of a series of Py-PDLGA samples prepared from a racemic mixture of D,L-glutamic acid. The process of pyrene excimer formation (PEF) was taken advantage of to probe changes in the conformation of α–helical Py-PLGA. Fluorescence Blob Model (FBM) analysis of the fluorescence decays of the Py-PLGA and Py-PDLGA constructs yielded the average number (<Nblob>) of glutamic acids located inside a blob, which represented the volume probed by an excited pyrenyl label. <Nblob> remained constant for randomly coiled Py-PDLGA but decreased from ~20 to ~10 glutamic acids for the Py-PLGA samples as GdHCl was added to the solution. The decrease in <Nblob> reflected the decrease in the local density of PLGA as the α–helix unraveled in solution. The changes in <Nblob> with GdHCl concentration was used to determine the change in Gibbs energy required to denature the PLGA α–helix in DMF. The relationship between <Nblob> and the local density of macromolecules can now be applied to characterize the conformation of macromolecules in solution.

scholarly journals Association Between a Genetic Variant Related to Glutamic Acid Metabolism and Coronary Heart Disease in Individuals With Type 2 Diabetes

JAMA ◽  
2013 ◽  
Vol 310 (8) ◽  
pp. 821 ◽  
Author(s):  
Lu Qi ◽  
Qibin Qi ◽  
Sabrina Prudente ◽  
Christine Mendonca ◽  
Francesco Andreozzi ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Coronary Heart Disease ◽  
Heart Disease ◽  
Glutamic Acid ◽  
Genetic Variant ◽  
Acid Metabolism

Thalidomide: Effects on Enzymes of Glutamic Acid Metabolism in Mice

Science ◽  
1964 ◽  
Vol 143 (3612) ◽  
pp. 1343-1344 ◽  
Author(s):  
E. Hirschberg ◽  
M. Osnos ◽  
S. Bryant ◽  
J. E. Ultmann
Keyword(s):  
Glutamic Acid ◽  
Acid Metabolism
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