Cell cycle patterns of thymidylate synthetase and 5,10-methylenetetrahydrofolate polyglutamates in cultured mouse hepatoma cells

Summary The regulation of thymidylate synthetase activity was investigated throughout the first cell cycle after release from an isoleucine block in synchronous cultures of mouse hepatoma (Hepa) cells. Activity in cell extracts increased with the onset of S phase and the increased activity was attributed to a parallel increase in enzyme concentration as determined by titration with tritiated fluorodeoxyuridylate. The polyglutamate chain length of reduced folate cofactors, which could also influence thymidylate synthetase activity, was unchanged.Acknowledgments. Supported by grant CA 22754, awarded by the National Cancer Institute, DHEW.     

Glutathione-related enzyme activities in pregnant rat liver

The levels of GSH-related enzyme activities during pregnancy were determined. A significant increase in Selenium-dependent GSH peroxidase and GSH S-transferase E activity was observed. A concomitant increase in gamma-glutamylcysteine synthetase was measured, which indicated an increased ability to synthesize the tripeptide.     

Purification and properties of glutamine synthetase I fromRhizobium sp. UMKL 20

Summary Glutamine synthetase I was purified fromRhizobium sp. UMKL 20 following polyethylene glycol precipitation. The enzyme had a subunit molecular weight of 58 kd. Apparent K_m values for ammonia and glutamate were 5.6 and 15.2 mM, respectively. Glutamine synthetase I activity was inhibited by several end products of glutamine metabolism. The purified enzyme was highly adenylylated (E _n ^– =8.5).Acknowledgment. I would like to thank Mr J. C. Lai for technical assistance. This work was carried out with the support of Vote F 153/79 from the University of Malaya.     

Substrate induced alterations in tryptophan pyrrolase activity in two mouse strains

Summary Total hepatic L-tryptophan 2,3-dioxygenase activity was studied in 2 mouse strains receiving i.p. injections of L-tryptophan. After a single injection, enzyme activity was increased in albino but not pigmented mice. After 3 injections, enzyme activity was reduced in both strains. This work was partially supported by grant No. 3726-22 from the Office of Research and Sponsored Programs, Wichita State University.     

Glutathione-related enzyme activities in pregnant rat liver

Summary The levels of GSH-related enzyme activities during pregnancy were determined. A significant increase in Selenium-dependent GSH peroxidase and GSH S-transferase E activity was observed. A concomitant increase in -glutamylcysteine synthetase was measured, which indicated an increased ability to synthesize the tripeptide.     

Evidence of protein kinase activity in 2 murine oncornaviruses]

A protein kinase activity has been detected in two strains of murine Oncornaviruses, MSV/MLV and EFV. This activity phosphorylates not only endogenous viral proteins but also exogenous substrates (histones and phosvitin). The stimulation of enzyme activity by detergents along with the increase of specific activity in viruses treated with trypsin during purification suggest that the enzyme is located in the viral particle.     

Control activities and regulation by the glucocorticoids of three urea-cycle enzymes in rat foetal liver: argininosuccinate synthetase, argininosuccinase and arginase (author's transl)]

The activity of three urea-cycle enzymes, argininosuccinate synthetase, argininosuccinase and arginase have been studied in the foetal and new-born liver of rats. The activity increases with regularity between 17.5 days of pregnancy and birth in control foetuses. The lack of corticosteroid from 18.5 days of pregnancy decreases the activity of argininosuccinate synthetase. After administration of cortisol (hydrocortisone), to these 18.5 day-old foetuses lacking of corticosteroids, both activities of argininosuccinate synthetase and arginase are enhanced.     

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     

Comparison of glutamate dehydrogenase and glutamine synthetase activities in the roots and aerial organs of an obligate halophyte: Suaeda maritima var. macrocarpa and a glycophyte: Phaseolus vulgaris, grown in presence of different concentration of NaCl]

The glutamate dehydrogenase and glutamine synthetase activities of an obligate halophyte, Suaeda maritima var. macrocarpa and a glycophyte. Phaseolus vulgaris are compared in function of salinity (increasing concentrations of NaCl) of the culturing solution. In culture, addition of NaCl stimulates glutamine synthetase activity and lowers glutamine dehydrogenase activity in the aerial organs and in the roots of Suaeda as opposed to what is observed in the glycophyte. Hence the obligatory halophily of Suaeda is related to an increase of the glutamine synthetase activity in a sal-trich medium corresponding to the stimulation of nitrate reductase and proteogenesis.     

Reactivation by glycerol and ethylene glycol of inactivated delta-aminolevulinic acid synthetase of Rhodopseudomonas spheroides.

Reactivation effects by glycerol and ethylene glycol of inactivated ALA synthetase of R. spheroids were observed. Accompanying the reactivation of the inactivated enzyme, Km value for PLP decreased to levels similar to those of the freshly prepared enzyme.     

Interstrain variation of murine arylsulfatase C.

A method has been developed for the assay of arylsulfatase C in tissue extracts containing arylsulfatases A and B. Significant variation of enzyme activity was observed among 26 inbred murine strains. Activity differences were apparent at all stages evaluated between 1 and 70 days postnatal age. Arylsulfatase C from representative high- and low-activity strains exhibited similar Michaelis constants, temperature optima, pH optima, thermostabilities and inhibitor profiles.     

Reactivation by glycerol and ethylene glycol of inactivatedδ-aminolevulinic acid synthetase ofRhodopseudomonas spheroides

Summary Reactivation effects by glycerol and ethylene glycol of inactivated ALA synthetase ofR. spheroides were observed. Accompanying the reactivation of the inactivated enzyme, K _m value for PLP decreased to levels similar to those of the freshly prepared enzyme.     

Development of oxidative metabolism in the non-innervated optic lobe of the chick.

Early removal of the optic cup of the chick embryo prevents innervation of the contralateral optic lobe. This reduces the rate of development od citrate synthetase. The posthatch increase of the level of this enzyme related to oxidative metabolism is not impaired by denervation of the chick optic lobe.     

Possible role of cell contact in the control of a differentiation program in Dictyostelium discoideum]

Synthesis of cAMP-phosphodiesterase falls at the end of the aggregation phase in Dictyostelium discoideum. Exogenous cAMP pulses, known to induce they synthesis of that enzyme during the course of the aggregation process, do not prevent the shut off of enzyme synthesis. Specific intercellular contacts which form at the end of aggregation seem to be required for the inhibition of enzyme synthesis.     

Superoxide dismutase and life span ofDrosophila melanogaster

Summary Comparison of superoxide dismutase activity in homogenates of wild and vestigial strains ofD. melanogaster revealed a lower enzyme activity in the short-living vestigial strain.Acknowledgments. We are indebted to Prof. M. Olszewska for giving us fly specimens. This work was partly supported by the project No. R. III. 13. 2. 4.     

Development of oxidative metabolism in the non-innervated optic lobe of the chick

Summary Early removal of the optic cup of the chick embryo prevents innervation of the contralateral optic lobe. This reduces the rate of development of citrate synthetase. The posthatch increase of the level of this enzyme related to oxidative metabolism is not impaired by denervation of the chick optic lobe.     

Interstrain variation of murine arylsulfatase C

Summary A method has been developed for the assay of arylsulfatase C in tissue extracts containing arylsulfatases A and B. Significant variation of enzyme activity was observed among 26 inbred murine strains. Activity differences were apparent at all stages evaluated between 1 and 70 days postnatal age. Arylsulfatase C from representative high- and low-activity strains exhibited similar Michaelis constants, temperature optima, pH optima, thermostabilities and inhibitor profiles.This work was supported in part by Biomedical Sciences Support Grant: HEW PHS RR 07030.     

Evolution et contrôle de l'activité de l'argininosuccinate synthétase,de l'argininosuccinase et de l'arginase du foie foetal de rat

Summary The activity of three urea-cycle enzymes, argininosuccinate synthetase, argininosuccinase and arginase have been studied in the ftal and new-born liver of rats. The activity increases with regularity between 17.5 days of pregnancy and birth in control foetuses. The lack of corticosteroid from 18.5 days of pregnancy decreases the activity of argininosuccinate synthetase. After administration of cortisol (hydrocortisone), to these 18.5-day-old foetuses lacking of corticosteroids, both activities of argininosuccinate synthetase and arginase are enhanced.

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Ce travail a été réalisé avec l'aide de la Délégation Générale à la Recherche Scientifique et Technique (contrat N^o 737 1148).     

Glutamine synthetase activity in subdivisions of brain of the shark, Squalus acanthias

Specific activity of glutamine synthetase in Squalus acanthias (spiny dogfish) central nervous system regions was highest in the cerebellum and lowest in the spinal cord. The levels of activity may relate to the excitability of each region by regulating the glutamate pool.     

庆大霉素产生菌GntB基因的克隆与转化

根据小单孢菌产生庆大霉素的生物合成机理，利用基因克隆方法从棘孢小单孢菌（Micromonospora echinospora）基因组中扩增出庆大霉素生物合成的关键酶基因—2-脱氧青蟹肌糖合成酶基因（GntB），并将其通过大肠杆菌／链霉菌穿梭质粒pIJ699转化原菌株，采用硫链丝菌素抗性基因启动子带动2-脱氧青蟹肌糖合成酶基因在棘孢小单孢菌细胞中实现了转化。