[38] Phosphohexokinase

Ling, Kuo-Huang; Byrne, William L.; Lardy, Henry A.

doi:10.1016/0076-6879(55)01042-2

Cited by 53 publications

(14 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…6-Phosphofructokinase was assayed by coupling to fructose-1,6-bisphosphate aldolase, triose isomerase, and a-glycerol-3-phosphate dehydrogenase (28). The assay mix contained 100 mM MES (2-[N-morpholine]ethanesulfonic acid)-Tris (pH 6.0), 5 mM dithiothreitol, 1 mM ATP, 2 mM MgCl2, 0.25 mM NADH, 5 U of rabbit muscle a-glycerol-3-phosphate dehydrogenase, 30 U of rabbit muscle triose isomerase, 1 U of trout muscle aldolase, and 10 plI of cell extract.…”

Section: Methodsmentioning

confidence: 99%

Pathway of glycogen metabolism in Methanococcus maripaludis

Ladapo

Whitman

1994

J Bacteriol

View full text Add to dashboard Cite

(80:20 [vol/vol]) in a 10-liter fermentor (54). The mineral medium was autoclaved under H2 plus C02 gas at a pressure of 35 kPa for 40 min. After cooling, the medium was sparged with H2 plus CO2. One hour before inoculation, 10 ml of a sterile solution of 20% Na2S 9H20 was added. The inoculum was 2 to 5% of the working volume and was in the exponential growth phase. During growth, the gas pressure inside the vessel was maintained at 140 kPa with an H2 plus CO2 flow rate of 9 to 18 liters h-1. The stirring rate was 240 to 300 rpm. An additional 10 ml of sterile 20% Na2S * 9H20) was added when the A660 of the culture reached 0.5. Cells were harvested in the early stationary phase with a Sharples continuous-flow centrifuge and stored under N2 gas at -20°C. In some experiments, 1-liter portions of the culture were anaerobically harvested throughout growth. A 1-liter stoppered bottle that had been sitting in an anaerobic chamber overnight was connected to the fermentor outlet with tubing and a syringe needle. The culture was forced into the bottle by the pressure in the fermentor. During this procedure, pressure inside the-bottle was vented by using a second syringe needle. Cells were then transferred to 500-ml centrifuge bottles in the anaerobic chamber and centrifuged at 11,000 x g for 20 min at 325

show abstract

Section: Methodsmentioning

confidence: 99%

Pathway of glycogen metabolism in Methanococcus maripaludis

Ladapo

Whitman

1994

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…(2) glucose-6-phosphate dehydrogenase (G6PDH), according to the method of Kornberg and H orecker [29]; (3) NADH-glutathione reductase (NADH-GR) and NADPH-glutathione reduc tase (NADPH-GR) by Racker's method [45]; (4) enzymes of the Embden-Meyerhoff-Parnas glycolytic cycle: hexokinase (HK), according to Crane and Sols [15]; phosphofructokinase (PFK), according to L ing et al [33]; aldolase (ALD), according to Bruns [6]; triosophosphate isomerase (TPI), according to Beisenherz [2]; phosphoglyceraldehyde phosphate dehydroge nase (GAPDH), according to Beisenherz et al [3]; enolase (ENOL), according to Bucher [7]; pyruvate kinase (PK), according to Bucher [50]; (6) adenosine triphosphatase (ATP-ase), according to H arvald et al [27]. Previous articles should be consulted for details concerning slight modifications of the techniques [22,34].…”

Section: Methodsmentioning

confidence: 99%

Hereditary Elliptocytosis

Torlontano¹,

Fontana²,

A³

et al. 1972

Acta Haematol

View full text Add to dashboard Cite

The of the erythrocyte biochemistry in 15 cases of hereditary elliptocytosis, shown and both before and after incubation with APHand an increase of G6PDH, NAPDH-GR, HK, PFK, ENOL, and LDH activities. A slight decrease in ALD and ATP-ase was also observed. The raised values of many enzymatic activities may be a consequence of hy-perhaemolysis and thus the presence of a young erythrocyte population containing an increased concentration of enzymes. The normal but low values of ATP-ase and the ALD deficiency may be the result of structural alterations of the erythrocyte membrane.

show abstract

“…Phosphofructokinase of rabbit muscle was prepared according to Ling, Byrne, and Lardy (1955), aldolase according to Taylor, Green, and Cori (1948 Cori, Slein, and Cori (1948). Glucose-6-phosphate dehydrogenase from yeast was prepared by a procedure identical to that used in a previous study (Bueding and MacKinnon, 1955a The concentration of hexose phosphates in the worm was determined in the following manner: the parasites were homogenized in 0.2 N-HCl (1 ml./100 worm pairs) in an all-glass homogenizer.…”

Section: Methodsmentioning

confidence: 99%

THE RELATIONSHIP BETWEEN INHIBITION OF PHOSPHOFRUCTOKINASE ACTIVITY AND THE MODE OF ACTION OF TRIVALENT ORGANIC ANTIMONIALS ON SCHISTOSOMA MANSONI

Bueding

Mansour

1957

British Journal of Pharmacology and Chemotherapy

View full text Add to dashboard Cite

The addition of purified mammalian phosphofructokinase to homogenates of Schistosoma mansoni increased the rate of lactic acid production from glucose and reversed the inhibition of glycolysis produced by low concentrations of trivalent organic antimonials. Neither mammalian phosphofructokinase nor trivalent antimonials affected the rate of lactic acid production from fructose-l: 6-diphosphate (HDP) by schistosome homogenates. Accordingly, in the schistosome, the rate of glycolysis of glucose is determined by the activity of phosphofructokinase.The aldolase of S. mansoni has a high requirement for HDP; relatively slight reductions in the concentration of this substrate below the optimum resulted in a sharp decline of aldolase activity. Therefore, decreased formation of HDP, due to inhibition of schistosome phosphofructokinase activity by antimonials, reduced the activity of aldolase and resulted in an inhibition of glycolysis of schistosome homogenates.Kinetic data revealed differences in the nature of the phosphofructokinase of S. mansoni and that of the enzyme catalysing the same reaction in the host. Exposure of schistosomes to low concentrations of potassium antimonyl tartrate or administration of subcurative doses of stibophen to the host resulted in an accumulation of the substrate (fructose-6-phosphate), and a reduction of the product (HDP) of the phosphofructokinase reaction, indicating that the activity of this enzyme was inhibited by antimonials in the intact parasite. It is concluded that inhibition of phosphofructokinase activity can account for the mechanism of the chemotherapeutic action of trivalent organic antimonials in schistosomiasis.

show abstract

[38] Phosphohexokinase

Cited by 53 publications

References 6 publications

Pathway of glycogen metabolism in Methanococcus maripaludis

Pathway of glycogen metabolism in Methanococcus maripaludis

Hereditary Elliptocytosis

THE RELATIONSHIP BETWEEN INHIBITION OF PHOSPHOFRUCTOKINASE ACTIVITY AND THE MODE OF ACTION OF TRIVALENT ORGANIC ANTIMONIALS ON SCHISTOSOMA MANSONI

Contact Info

Product

Resources

About