The effect of β-N-oxalylamino-l-alanine on glutamine synthetase activity and the transport of d-3 H-aspartate in rat brain in vitro

1994 ◽  
Vol 22 (1) ◽  
pp. 15S-15S
Author(s):  
KEVINA B. DOORTY ◽  
GETHIN J. McBEAN
Keyword(s):  
Glutamine Synthetase ◽  
Rat Brain ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity

Assessment of glutamine synthetase activity by [13N]ammonia uptake in living rat brain

Synapse ◽  
2014 ◽  
Vol 69 (1) ◽  
pp. 26-32 ◽  
Author(s):  
Sotaro Momosaki ◽  
Miwa Ito ◽  
Misato Tonomura ◽  
Kohji Abe
Keyword(s):  
Glutamine Synthetase ◽  
Rat Brain ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Ammonia Uptake

Age-Related Changes in Glutamine Synthetase Activity of Rat Brain, Liver and Heart

Gerontology ◽  
1985 ◽  
Vol 31 (2) ◽  
pp. 95-100 ◽  
Author(s):  
H. Cao Danh ◽  
M. Strolin Benedetti ◽  
P. Dostert
Keyword(s):  
Glutamine Synthetase ◽  
Rat Brain ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Age Related ◽  
Age Related Changes

In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei

2011 ◽  
Vol 39 (1) ◽  
pp. 259-262 ◽  
Author(s):  
Laia Pedro-Roig ◽  
Mónica Camacho ◽  
María José Bonete
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Metabolism ◽  
Model Organism ◽  
Methanogenic Archaea ◽  
Ammonium Assimilation ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Haloferax Mediterranei ◽  
Pii Proteins

Haloferax mediterranei is an extreme halophilic micro-organism belonging to the Archaea domain that was isolated from the Santa Pola solar salterns (Alicante, Spain) in 1983. The biochemistry of the proteins involved in nitrogen metabolism is being studied, but the knowledge of their regulation is very scarce at present. The PII superfamily is constituted by major regulators of nitrogen metabolism, which are widespread in prokaryotic and eukaryotic organisms. These trimeric proteins (12 kDa per subunit) have in Escherichia coli long been known to regulate GS (glutamine synthetase) activity via its adenylyltransferase/adenylyl-removing enzyme and, more recently, to be able to interact directly with this enzyme in methanogenic archaea. We have tested the possible role of PII proteins in the regulation of ammonium assimilation in our model organism and the results clearly indicate that the direct influence of GS by PII proteins can also take place in halophilic archaea, starting with the comprehension of nitrogen regulation in those organisms.

scholarly journals Glutamine synthetase in muscle and kidney

1970 ◽  
Vol 119 (2) ◽  
pp. 145-156 ◽  
Author(s):  
Khalid Iqbal ◽  
J. H. Ottaway
Keyword(s):  
Skeletal Muscle ◽  
Glutamine Synthetase ◽  
Synthetase Activity ◽  
Glutamine Synthetase Activity ◽  
Optimum Conditions ◽  
Muscle Enzyme ◽  
Tissue Extracts ◽  
Kidney Enzyme

1. Glutamine synthetase activity has been determined in extracts of rat cardiac and skeletal muscle and kidney, after treatment to ensure that the rate of synthesis was proportional to time of incubation and to amount of extract added. The activity was measured by two methods, with hydroxylamine as substrate. 2. No activity was detected in rat heart extract by either method. The activity in skeletal muscle was of the order of 20μmol of glutamylhydroxamate synthesized/h per g of tissue under optimum conditions. The activity in kidney extracts was 180μmol/h per g of tissue when measured as ferric hydroxamate. 3. The activity in both skeletal-muscle and kidney extracts was inhibited by Pi. The inhibition is competitive for the muscle enzyme, with a Ki of 12mm. For the kidney enzyme the inhibition is non-competitive, and less marked. Possible enzyme mechanisms that would lead to these types of inhibition are discussed. 4. Several observations are reported that suggest that the enzymes from muscle and kidney are not identical. 5. Growth hormone, either in vivo or in vitro, did not affect the measured glutamine synthetase activity of tissue extracts.

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