Glutathione synthetase deficiency

Glutathione (GSH), one of the most important antioxidants in the eukaryotic organism, is synthesized in a two-step procedure where the last step is catalysed by the enzyme glutathione synthetase (GSS). GSS deficiency is inherited autosomal recessively, and patients with this disease can be divided into three groups, according to their clinical phenotype. Mildly affected patients have mutations affecting the stability of the enzyme, causing a compensated haemolytic anaemia; moderately affected patients have, in addition, metabolic acidosis; and severely affected patients also develop neurological defects and show increased susceptibility to bacterial infections. Moderately and severely affected patients have mutations that compromise the catalytic properties of the enzyme. 5-Oxoprolinuria appears in all three groups, but is more pronounced in the two latter groups. Today, no cure can be offered these patients; they are given vitamins C and E to boost their antioxidant levels, and bicarbonate to correct metabolic acidosis.Received 20 April 2005; received after revision 19 May 2005; accepted 20 May 2005     

Occurrence of oxalyl-CoA synthetase in Indian pulses

Summary The presence of oxalyl-CoA synthetase was observed in common edible pulses. Excepting in chick pea, the changes in oxalyl-CoA synthetase activity of winter pulses proceeded in stages. The enzyme remained more active in late strains than in early strains of winter pulses. Unlike the activity of the enzyme in winter pulses, that in summer pulses behaved differently.     

Erythrocyte glucose-6-phosphate dehydrogenase deficiency and thalassemia

Résumé L'activité de la glucose-6-phosphate déhydrogènase était normale dans les érythrocytes obtenus de sujets atteints de Thalassémie (majeure ou mineure) d'Hémoglobine E - Thalassémie et dans des érythrocytes contenant une variété d'hémoglobines anormales. Chez trois des six sujets atteints d'Hémoglobine H - Thalassémie, la glucose-6-phosphate déhydrogènase était absente.     

Immunohistochemical localization of glutamine synthetase in human liver

Glutamine synthetase (GS) of human liver was recognized with a polyclonal antibody to pig brain GS, but failed to stain with an antibody against rat liver GS. Using the latter antibody GS of human liver was shown to be localized within small rings of 1 to 3 hepatocytes surrounding the terminal hepatic venules. This pattern was analogous to that seen in rat and mouse liver.     

Immunohistochemical localization of glutamine synthetase in human liver

Glutamine synthetase (GS) of human liver was recognized with a polyclonal antibody to pig brain GS, but failed to stain with an antibody against rat liver GS. Using the latter antibody GS of human liver was shown to be localized within small rings of 1 to 3 hepatocytes surrounding the terminal hepatic venules. This pattern was analogous to that seen in rat and mouse liver.     

Heme structure in cooperative and noncooperative hemoglobins: study by resonant Raman diffusion]

The modifications of heme sites of hemoglobin, which should occur upon apoprotein alterations (responsible for variations of oxygen affinity), have been examined by Resonnant Raman scattering. The oxygenated (R) and deoxygenated (T) shape of apoprotein do not modify the heme states. The spectral differences between these forms are essentially due to the presence or the absence of the sixth ligand.     

Development of gamma-glutamylcysteine synthetase and oxoprolinase in rat kidney.

gamma-Glutamylcysteine synthetase is present in barely detectable amounts in foetal kidney. Its activity starts to increase in postnatal life. In contrast, oxoproline is already found in significant quantities in the foetal tissue. Both enzymes show marked elevation in activities during the weaning period.     

Activity of cytidine triphosphate synthetase in normal and neoplastic tissues

Résumé L'activité de la synthétase CTP dans différents tissus normaux et cancéreux a été étudiée. Les résultats indiquent qu'elle est élevée dans les tissus en prolifération.     

Chitin synthetase activity and inhibition in different insect microsomal preparations

Summary To facilitate massive screening and for structure-activity relationship studies of chitin synthesis inhibitors, methods to obtain the chitin synthetase (CS) containing microsomal fraction from the postmitochondrial supernatant were examined. Compared with fractionation by differential centrifugation, the CaCl₂ precipitate yielded the most active CS preparation. Acidification (pH 5.6) and polyethylene glycol 8000 (5%) treatments resulted in relatively low CS activity. Inhibitory effects were detected with polyoxin-D and 1-geranyl-2-methyl benzimidazole, a novel CS inhibitor, but not with benzoylphenyl ureas.     

The polyphosphate synthetase of Saccharomyces cerevisiae]

The polyphosphate-synthetase, isolated from a homogenate of phosphate starved cells, catalyses the synthesis of linear polyphosphates from orthophosphate. It is localized in the membrane fraction which deposits between 400 and 1000 X g; its optimal pH is 7.1; its KM toward orthophosphate is 4.0 X 10(-4) M; ATP stimulates the reaction. The enzyme synthezises especially polyphosphates with short chain length.     

Inhibition of prostaglandin synthetase by psychotropic drugs

Zusammenfassung Psychopharmaka mit neuroleptischer, antidepressiver und/oder tranquillisierender Wirkung, die eine trizyklische Struktur besitzen, hemmen in vitro dosisabhängig die Prostaglandin-Synthetase, welche aus Ochsensamenblase isoliert wurde. Hingegen weist das Neuroleptikum Haloperidol, das sich strukturell von den anderen untersuchten Präparaten wesentlich unterscheidet, kaum einen solchen Effekt auf. Die pharmakologische Bedeutung dieser Befunde wird diskutiert.     

Silymarin,an inhibitor of prostaglandin synthetase

Summary Silybin (I), silydianin (II) and silychristin (III), the main constituents of silymarin, inhibit the formation of prostaglandins in vitro. The inhibition is log-linearly dependent on the concentration of the effectors.F. Fiebrich, Thesis, University of Vienna 1977.H. Koch, Dt. ApothZtg118, 1844 (1978); reported in part at the Colloquium Pharmaceuticum in Münster, 21st November 1978.     

Acetyl-coenzyme A synthetase (AMP forming)

Acetyl-coenzyme A synthetase (AMP forming; Acs) is an enzyme whose activity is central to the metabolism of prokaryotic and eukaryotic cells. The physiological role of this enzyme is to activate acetate to acetyl-coenzyme A (Ac-CoA). The importance of Acs has been recognized for decades, since it provides the cell the two-carbon metabolite used in many anabolic and energy generation processes. In the last decade researchers have learned how carefully the cell monitors the synthesis and activity of this enzyme. In eukaryotes and prokaryotes, complex regulatory systems control acs gene expression as a function carbon flux, with a second layer of regulation exerted posttranslationally by the NAD⁺/sirtuin-dependent protein acetylation/deacetylation system. Recent structural work provides snapshots of the dramatic conformational changes Acs undergoes during catalysis. Future work on the regulation of acs gene expression will expand our understanding of metabolic integration, while structure/function studies will reveal more details of the function of this splendid molecular machine.Received 4 December 2003; received after revision 2 March 2004; accepted 16 March 2004     

Glutamine synthetase activity during mouse brain development

The specific activity of glutamine synthetase (GS) in mouse brain was 2-fold higher in the olfactory bulbs than in other regions. After birth, the specific activity of GS increased more rapidly in medulla oblongata and in olfactory bulbs, than in cerebral and cerebellar cortex. The activity of GS in primary cultures of brain hemispheres increased more slowly than in homogenates of whole brains. However, when astroblasts were treated in vitro with glucocorticoids or mouse brain extracts, GS activity reached 4 times the level measured in the homogenate of an adult mouse brain. We conclude that levels of GS activity may relate to the maturation of astrocytes, and propose that GS may be used as a marker of astrocytic maturation.     

Glutamine synthetase activity during mouse brain development

Summary The specific activity of glutamine synthetase (GS) in mouse brain was 2-fold higher in the olfactory bulbs than in other regions. After birth, the specific activity of GS increased more rapidly in medulla oblongata and in olfactory bulbs, than in cerebral and cerebellar cortex. The activity of GS in primary cultures of brain hemispheres increased more slowly than in homogenates of whole brains. However, when astroblasts were treated in vitro with glucocorticoids or mouse brain extracts, GS activity reached 4 times the level measured in the homogenate of an adult mouse brain. We conclude that levels of GS activity may relate to the maturation of astrocytes, and propose that GS may be used as a marker of astrocytic maturation.     

Activity of rabbit heart on thromboxane synthetase]

The soluble and microsomal fractions of Rabbit myocardium are not able to induce the synthesis of thromboxanes. On the contrary, they inhibit the thromboxane synthetase of various sources. The chemical structure of the active constituent responsible for this activity is not yet known: it is probably neither of an enzymatic nature, nor a protein of high molecular weight.     

Silymarin, an inhibitor of prostaglandin synthetase.

Silybin (I), silydianin (II) and silychristin (III), the main constituents of silymarin, inhibit the formation of prostaglandins in vitro. The inhibition is log-linearly dependent on the concentration of the effectors.