Interrelated Effects of Calcium and Sulfhydryl Reagents on Renal Phosphate-Activated Glutaminase

2015 ◽  
pp. 156-160 ◽  
Author(s):  
Elling Kvamme ◽  
Bj�rg Roberg ◽  
Liv Johansen ◽  
Ingeborg Aa. Torgner
Keyword(s):  
Sulfhydryl Reagents ◽  
Phosphate Activated Glutaminase

Inactivation of Streptococcal Bacteriophage by Sulfhydryl Reagents.

1963 ◽  
Vol 114 (3) ◽  
pp. 822-826 ◽  
Author(s):  
D. Kessler ◽  
R. M. Krause
Keyword(s):  
Sulfhydryl Reagents

scholarly journals Studies on Human Hemoglobin Treated with Various Sulfhydryl Reagents

1966 ◽  
Vol 241 (1) ◽  
pp. 241-248
Author(s):  
John Fuller Taylor ◽  
Eraldo Antonini ◽  
Maurizio Brunori ◽  
Jeffries Wyman
Keyword(s):  
Human Hemoglobin ◽  
Sulfhydryl Reagents

Fusicoccin antagonizes the effect of sulfhydryl reagents in inducing an oxidative burst inElodea densaleaves

1995 ◽  
Vol 129 (4) ◽  
pp. 1049-1050 ◽  
Author(s):  
Mario Bellando ◽  
Silvano Sacco ◽  
Pietro Rocco ◽  
Maria Teresa Marré ◽  
Francesco Albergoni
Keyword(s):  
Oxidative Burst ◽  
Sulfhydryl Reagents

scholarly journals The regulation of phosphate-activated glutaminase activity and glutamine metabolism in the streptozotocin-diabetic rat

1984 ◽  
Vol 224 (1) ◽  
pp. 207-214 ◽  
Author(s):  
M Watford ◽  
E M Smith ◽  
E J Erbelding
Keyword(s):  
Drinking Water ◽  
Small Intestine ◽  
Glutamine Metabolism ◽  
Diabetic Rat ◽  
Complete Suppression ◽  
Chemically Induced ◽  
Phosphate Activated Glutaminase ◽  
Kidney Liver ◽  
Nh4cl Solution ◽  
Glutaminase Activity

The activity of phosphate-activated glutaminase was increased in the kidney, liver and small intestine of rats made diabetic for 6 days with injection of streptozotocin (75 mg/kg body wt.). Insulin prevented this increase in all three tissues. Treatment with NaHCO3, to correct the acidosis that accompanies diabetes, prevented the increase in renal glutaminase activity, but not that in liver or small intestine. Chemically induced acidosis (NH4Cl solution as drinking water) or alkalosis (NaHCO3 solution as drinking water) increased and decreased, respectively, glutaminase activity in the kidney, but were without significant effect on the activity in liver and small intestine. The increase in glutaminase activity in the small intestine during diabetes was due to an overall increase in the size of this organ, and was only detectable when activity was expressed in terms of whole organ, not mucosal scrapings or isolated enterocytes. Prolonged diabetes (40 days) resulted in an even greater increase in the size and glutaminase activity of the small intestine. Despite this marked increase in capacity for glutamine catabolism, arteriovenous-difference measurements showed a complete suppression of plasma glutamine utilization by the small intestine during diabetes, confirming the report by Brosnan, Man, Hall, Colbourne & Brosnan [(1983) Am. J. Physiol. 235, E261-E265].

Acetylsalicylic acid hydrolase of gastric mucosa.

1978 ◽  
Vol 234 (6) ◽  
pp. E606
Author(s):  
J G Spenney
Keyword(s):  
Gastric Mucosa ◽  
Enzymatic Activity ◽  
Acetylsalicylic Acid ◽  
Sodium Dodecyl ◽  
Sodium Cholate ◽  
Acid Hydrolase ◽  
Sulfhydryl Reagents ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate

Acetylsalicylic acid hydrolase activity of rabbit fundic gastric mucosa has been isolated from the soluble 100,000 X g supernate. The enzymatic activity was partially purified by ammonium sulfate precipitation. The Km for acetylsalicylate was 2 mM and pH optimum was 8.6. The activity was insensitive to ionic strength, slightly inhibited by inclusion of 100 mM Cl-, and demonstrated no requirement for Ca2+ or Mg2+. Acetylsalicylic acid esterase was markedly inhibited by sodium cholate and sodium dodecyl sulfate. The enzyme was insensitive to sulfhydryl reagents with the exception of p-chloromercuribenzenesulfonic acid, which markedly inhibited the enzyme. Diisopropyl fluorophosphate (DFP) inhibited enzymatic activity with a Ki of 9 X 10(-9)M. Eserine was also inhibitory with a Ki of 0.25 mM. Inhibition by DFP at low concentration and by eserine at millimolar concentrations suggests that this enzyme is related to the group of aliphatic esterases. Identification of potent inhibitors will enable studies to define the role of this enzyme with the use of experimental preparations in which systemic toxicity can be avoided.

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