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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The behaviour and properties of membrane-bound GAPDH of rabbit reticulocytes were investigated. 2. The bound GAPDH is more resistant to inactivation by KCl than the soluble enzyme (allotopy). 3. The bound enzyme is released by electrolytes. This effect does not only depend on the ionic strength but additionally on the kind of ions, pH-value and protein concentration. 4. A comparison of the releasing effect of NAD analogues shows the necessity of the 5'-AMP moiety in the structure of the effector. 5. The represented results demonstrate the specifity of the GAPDH-membrane binding in rabbit reticulocytes.
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PMID:Further characterization of the association of glyceraldehyde-3-phosphate dehydrogenase with reticulocyte membranes. 0 Aug 80

Incubation of HeLa cells with [32P]orthophosphate results in more rapid labeling of the gamma-phosphorus of ATP than of the intracellular pool of orthophosphate. The specific radioactivity of ATP equals that of extracellular orthophosphate after 2 h of incubation. A similar pattern of labeling is seen with human erythrocytes when incubated at physiological concentrations of orthophosphate (2 mM) and pH 7.4-7.8. At lower pH, 6.8-7.2, the rate of orthophosphate uptake increases and exceeds the rate of labeling of ATP. These data are explained by the existence of a primary system for ATP uptake which involves the mediation of membrane-bound glyceraldehyde-3-phosphate dehydrogenase. Phosphate first enters the cell as 1,3-diphosphoglyceric acid, is then transferred to ATP, and then enters the intracellular orthophosphate pool. At lower pH monovalent orthophosphate also enters the erythrocyte by a process not involving glyceraldehyde-3-phosphate dehydrogenase.
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PMID:Mode of orthophosphate uptake and ATP labeling by mammalian cells. 0 42

The effect of estradiol-17 beta on the activities of glycolytic enzymes from female rat brain was studied. The following enzymes were examined: hexokinase (HK, EC 2.7.1.1), phosphofructokinase (PFK, EC 2.7.1.11), aldolase (EC 4.1.2.13), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), phosphoglycerate kinase (EC 2.7.2.3), phosphoglycerate mutase (EC 2.7.5.3), enolase (EC 4.2.1.11) and pyruvate kinase (PK, EC 2.7.1.40). The activities of HK (soluble and membrane-bound), PFK and PK were increased after 4 h of hormone treatment, while the others remained constant. The changes in activity were not seen in the presence of actinomycin D. The significant rise of the activities of the key glycolytic enzymes was also observed in the cell culture of mouse neuroblastoma C1300 treated with hormone. Only three of the studied isozymes, namely, HKII, B4 and K4 were found to be estradiol-sensitive for HK, PFK and PK, respectively. The results obtained suggest that rat brain glycolysis regulation by estradiol is carried out in neurons due to definite isozymes induction.
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PMID:Rat brain glycolysis regulation by estradiol-17 beta. 153 2

Activity of membrane-bound enzymes, passive penetration of ions in dose-dependent loading with cholesterol, effect of cholesterol high concentrations on the metabolic patterns in cytosol, viscosity of cell suspension were studied in erythrocytes. Passive cotransport of H+ and Cl- ions via erythrocyte membrane was increased with augmentation in viscosity of the cell suspension. After loading with cholesterol activity of acetylcholinesterase was increased while ATPase and glyceraldehyde-3-phosphate dehydrogenase activities were decreased. The alteration in the enzymatic activity occurred on those sides of the membranes, where these enzymes were localized. Activity of lactate dehydrogenase was decreased in cytoplasm of erythrocytes. The alterations detected may be important in development of ischemic syndrome in hyperlipoproteinemia.
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PMID:[Activity of membrane-bound enzymes, indices of metabolism in the cytoplasm and various physico-chemical properties of erythrocytes with increased cholesterol level]. 293 99

Glycosomes are intracellular, membrane-bound microbody organelles of trypanosomes and leishmania. Nine glycolytic enzymes are the major protein components of the glycosomes of Trypanosoma brucei long-slender bloodstream forms. Glycosomal proteins are believed to be synthesized in the cytoplasm and inserted across the glycosomal membrane posttranslationally. We have developed an in vitro protein import assay for the study of glycosomal biogenesis in T. brucei. All nine glycosomal glycolytic enzymes were detectable by immunoprecipitation and gel analysis of radiolabeled products derived from in vitro translation of total mRNA. Radiolabeled translational products were incubated with purified glycosomes isolated from bloodstream forms and digested with protease to remove proteins not imported into glycosomes. Gel analysis of reisolated glycosomes revealed that glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) and 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) were apparently imported intact into the glycosome. Specificity of the protein import assay was verified by using translational products derived from cloned genes encoding T. brucei glycosomal PGK and its 95% homologous cytosolic isozyme. Glycosomal PGK was inserted into the glycosome in vitro with a 27.6% efficiency, but no imported cytosolic PGK was detectable. Preliminary data suggest that certain sequences between the N terminus and residue 123 may be important for import of glycosomal PGK. Our assay, combined with the potential use of genetically altered substrate proteins, may provide the opportunity to explore the recognition systems involved in glycosome biogenesis.
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PMID:Biogenesis of glycosomes of Trypanosoma brucei: an in vitro model of 3-phosphoglycerate kinase import. 328 31

Glycosomes, the microbodies of Trypanosoma brucei, contain a number of enzymes involved in glucose and glycerol metabolism. The biogenesis of three of these enzymes has been studied. Aldolase, D-glyceraldehyde-3-phosphate dehydrogenase and NAD-linked glycerol-3-phosphate dehydrogenase are all synthesized in the cytosol on free rather than on membrane-bound polysomes. In vitro, as well as in vivo, these polypeptides are synthesized at their mature size, and no evidence was found for any processing upon entry into the glycosomes. Continuous and pulse-chase labelling experiments with procyclic trypomastigotes revealed that the enzymes have a half-life in the cytosol of approximately 3 min or less, and then turn over rapidly in the glycosomes, with half-lives as short as 30 min.
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PMID:Biogenesis of the glycosome in Trypanosoma brucei: the synthesis, translocation and turnover of glycosomal polypeptides. 360 83

1. Guinea-pig erythrocytes contain half the activity of the enzyme glyceraldehyde-3-phosphate dehydrogenase (G3PD) present in human cells. About 60% of their total activity is membrane-bound. 2. Rabbit erythrocytes also contain half the amount of the enzyme of human red cells. The distribution of G3PD in rabbit cells, however, is similar to that of human cells with 70% of the enzyme being membrane-bound. 3. Mouse erythrocytes contain about two-thirds of G3PD activity present in human cells. All their enzyme activity is present in membrane-free hemolysate. 4. Non-human erythrocyte membrane proteins, in addition, have relatively greater amount of band 2.1, lack band 2.2, have a more heterogenous band 3 than its human counterpart, and have overlapping bands 4.1 and 4.2.
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PMID:Comparative distribution of glyceraldehyde 3-phosphate dehydrogenase activity in human, guinea-pig, rabbit and mouse erythrocytes. 366 31

The relative effectiveness of oxidizing (.OH, H2O2), ambivalent (O2-) and reducing free radicals (e- and CO2-) in causing damage to membranes and membrane=bound glyceraldehyde-3-phosphate dehydrogenase of resealed erythrocyte ghosts has been determined. The rates of damage to membrane-bound glyceraldehyde-3-phosphate dehydrogenase (R(enz)) were measured and the rates of damage to membranes (R(mb)) were assessed by measuring changes in permeability of the resealed ghosts to the relatively low molecular weight substrates of glyceraldehyde-3-phosphate dehydrogenase. Each radical was selectively isolated from the mixture produced during gamma-irradiation, using appropriate mixtures of scavengers such as catalase, superoxide dismutase and formate. .OH, O2- and H2O2 were approximately equally effective in inactivating membrane-bound glyceraldehyde-3-phosphate dehydrogenase, while e- and CO2- were the least effective. R(enz) values of O2- and H2O2 were 10-times and of .OH 15-times that of e-. R(mb) values were quite similar for e- and H2O2 (about twice that of O2-), while that of .OH was 3-times that of O2-. Hence, with respect to R(mb): .OH greater than e- = H2O2 greater than O2-, and with respect to R(enz): .OH greater than O2- = H2O2 much greater than e-. The difference between the effectiveness of the most damaging and the least damaging free radicals was more than 10-fold greater in damage to the enzyme than to the membranes. Comparison between H2O2 added as a chemical reagent and H2O2 formed by irradiation showed that membranes and membrane-bound glyceraldehyde-3-phosphate dehydrogenase were relatively inert to reagent H2O2 but markedly susceptible to the latter.
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PMID:The relative effectiveness of .OH, H2O2, O2-, and reducing free radicals in causing damage to biomembranes. A study of radiation damage to erythrocyte ghosts using selective free radical scavengers. 626 Jan 72

Binding of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase [GAPDHase; D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating EC 1.2.1.12], to the cytoplasmic segment of band-3 protein in the erythrocyte (RBC) membrane has been examined by electron paramagnetic resonance (EPR) and saturation transfer EPR (ST-EPR) spectroscopies. GAPDHase, which was isolated from rabbit muscle and labeled with the resolution-enhancing deuterated N-(15N-1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)maleimide spin label ([15N,2H]MSL), showed the same binding specificity for the transmembrane band-3 protein of human erythrocyte membranes as reported for unlabeled GAPDHase from human RBC. Experimental EPR lineshapes from soluble and membrane-bound enzymes were analyzed by direct stimulation of spectra and indicated a structural alteration of the bound GAPDHase in the vicinity of the spin label, which was attached covalently to the active-site cysteine-149 residue. A rigorous theoretical analysis of the ST-EPR spectra of soluble and membrane-bound enzyme is presented and utilized in conjunction with model system analysis to demonstrate that the motion of membrane-bound GAPDHase could be characterized by an effective isotropic rotational correlation time of 20 microseconds. This indicated that the GAPDHase--band-4 complex exhibits motional freedom relative to the membrane-spanning segment of the band-3 protein or the RBC. The double substituted spin label [15N,2H]MSL affords gains in sensitivity and resolution that permit studies of membrane-bound enzymes at physiological levels and quantitative simulations of the EPR and ST-EPR lineshapes with reasonable computation times.
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PMID:Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance. 627 85

ATP stimulates Na transport into inside-out vesicles (IOVs) made from human red cell membranes; strophanthidin inhibits the ATP-stimulated transport. The substrates for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) (glycolytic enzymes bound to the cytoplasmic surface of the red cell membrane) also stimulate Na transport into IOVs without added ATP. The elution of GAPDH from the membranes prevents the stimulation by the substrates, but not by exogenous ATP. Hexokinase plus glucose (agents that promote breakdown of ATP) prevent stimulation of Na transport by exogenous ATP but not by the substrates for GAPDH and PGK. [32P]orthophosphate is incorporated into a membrane-bound organic phosphate compound shown chromatographically to be ATP. The level of membrane-bound ATP is decreased when Na is added, and this decrease is inhibited by strophanthidin. When further synthesis of [32P]ATP is blocked by the addition of unlabeled orthophosphate, all of the membrane-bound [32P]ATP is dissipated by the addition of Na. From these observations it was concluded that membrane-bound glycolytic enzymes synthesize ATP and deposit it in a membrane-associated compartment from which it is used by the Na/K pump.
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PMID:Membrane-bound ATP fuels the Na/K pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes. 627 95


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