Hysteresis and conformational drift of pressure-dissociated glyceraldehydephosphate dehydrogenase

Biochemistry ◽  
1989 ◽  
Vol 28 (5) ◽  
pp. 2144-2153 ◽  
Author(s):  
Kancheng Ruan ◽  
Gregorio Weber
Keyword(s):  
Glyceraldehydephosphate Dehydrogenase

scholarly journals Inhibition of Fructolysis in Boar Spermatozoa by the Male Antifertility Agent (S)-a-Chlorohydrin

1982 ◽  
Vol 35 (6) ◽  
pp. 595 ◽  
Author(s):  
Denise Stevenson ◽  
A RJones
Keyword(s):  
Oxidative Metabolism ◽  
Inhibitory Activity ◽  
Energy Charge ◽  
Substrate Level Phosphorylation ◽  
Charge Potential ◽  
Substrate Level ◽  
Glyceraldehydephosphate Dehydrogenase ◽  
Fructose 1,6 Bisphosphate ◽  
Boar Spermatozoa

The (S)-isomer of the male antifertility agent IX-chlorohydrin strongly inhibited the oxidative metabolism of fructose by boar spermatozoa in vitro. The result of this action, which has been deduced to be an inhibition of glyceraldehydephosphate dehydrogenase, caused an accumulation of fructose- 1,6-bisphosphate and the triosephosphates, and a decrease in substrate-level phosphorylation with a concomitant lowering of the energy charge potential of the spermatozoa. The (R)-isomer of IX-chlorohydrin had no inhibitory activity on fructolysis.

Carbohydrate metabolism in Acanthamoeba castellanii. 1. The activity of key enzymes and [14C]-glucose metabolism

1973 ◽  
Vol 19 (9) ◽  
pp. 1131-1136 ◽  
Author(s):  
Lansing M. Prescott ◽  
Harold E. Hoyme ◽  
Darlene Crockett ◽  
Elena Hui
Keyword(s):  
Carbohydrate Metabolism ◽  
Citrate Synthase ◽  
Tricarboxylic Acid Cycle ◽  
Fumarate Hydratase ◽  
Acanthamoeba Castellanii ◽  
Tricarboxylic Acid ◽  
Pentose Phosphate ◽  
Acid Cycle ◽  
Key Enzymes ◽  
Glyceraldehydephosphate Dehydrogenase

The specific activities of a number of the key enzymes involved in carbohydrate metabolism in Acanthamoeba castellanii (Neff clone I–12) have been determined. The following Embden–Meyerhof and pentose phosphate pathway enzymes were present: glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokinase, phosphofructokinase, hexose diphosphatase, aldolase, glyceraldehydephosphate dehydrogenase, pyruvate kinase, and pyruvate-phosphate dikinase. The following tricarboxylic acid cycle enzymes were also found: citrate synthase, aconitase, isocitrate dehydrogenase, succinate dehydrogenase, fumarate hydratase, and malate dehydrogenase. The degradation of glucose-U-14C to 14CO2 was examined. Aerobic 14CO2 production from glucose-U-14C was 3.4-fold greater than anaerobic production. The data provide further evidence that the Embden–Meyerhof, pentose phosphate, and tricarboxylic acid cycle pathways are probably functional in A. castellanii.

Adaptive Potentials of Skeletal Muscle in Young and Aging Rats

2001 ◽  
Vol 11 (s1) ◽  
pp. S3-S8 ◽  
Author(s):  
Dirk Pette ◽  
Dejan Škorjanc
Keyword(s):  
Citrate Synthase ◽  
Relative Concentration ◽  
Low Frequency ◽  
Glycolytic Enzyme ◽  
Type I ◽  
Positive Type ◽  
Frequency Stimulation ◽  
Glyceraldehydephosphate Dehydrogenase ◽  
Aging Muscle ◽  
Type I Fibers

We compared responses of the fast extensor digitorum longus (EDL) and tibialis anterior (TA) muscles in young (15-week) and aging (101-week) male Brown Norwegian rats to 50 days of chronic low-frequency stimulation (CLFS, 10 Hz, 10 hours/day). After 50 days of CLFS, the EDL muscles of the young (22-week) and aging (108-week) rats displayed similar increases in type IIA fibers, relative concentration of myosin heavy chain MHCIIa, elevations in mitochondrial citrate synthase and 3-hydroxyacyl-CoA dehydrogenase activities, and similar decreases in glycolytic enzyme activities (glyceraldehydephosphate dehydrogenase, lactate dehydrogenase). TA muscle in young rats contained a few cytochrome c oxidase negative (COX−) type I fibers. Their number was ~2-fold elevated by CLFS. Conversely, aging muscle, which contained a slightly higher amount of COX− fibers than young TA muscle, responded to CLFS with a significant decrease in COX− fibers. The appearance of small COX-positive type I fibers in stimulated aging muscle indicated that regenerating type I fibers “diluted” the COX-deficient fiber population.

Sign in / Sign up

Export Citation Format

Share Document