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Results for “GLYCERALDEHYDEPHOSPHATE DEHYDROGENASE”

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At least 19 recordsLinked to original sources

PubMedDate not supplied

[Comparative immunological study of glyceraldehydephosphate dehydrogenase in Enterobacteriaceae: contribution of an anti-glyceraldehydephosphate dehydrogenase antiserum of Enterobacter intermedium].

A comparative immunological study of glyceraldehyde-3-phosphate dehydrogenase among Enterobacteriaceae was carried out with an antiserum against Enterobacter intermedium G-3-PDH. Results of immunodiffusion experiments and microcomplement fixation studies showed E. intermedium to be a homogeneous species. The genera Enterobacter and Escherichia were found to be quite heterogeneous.

Complement Fixation Tests↗

PubMed1989

Hysteresis and conformational drift of pressure-dissociated glyceraldehydephosphate dehydrogenase.

Pressure dissociation of yeast glyceraldehydephosphate dehydrogenase (GAPDH) was studied by fluorescence spectroscopy. Observations in the range of -5 to 30 degrees C indicate that monomer association into the tetramer proceeds with an enthalpy change of -14 kcal mol-1 and a large increase in entropy which at 25 degrees C amounts to 18 kcal mol-1. The large conformational drift and the low-temperature stability of the tetramer recovered after decompression facilitated a comparison of its properties with those of the native tetramer. Significant differences in absorption and fluorescence-excitation polarization spectra, yield of tryptophan fluorescence, and binding of anilinonaphthalenesulfonate and NADH were observed. At 0 degree C the standard free energies of association of the monomers into the native and drifted tetramers were respectively -32 and -29 kcal mol-1. The volume change upon association measured from the pressure span of the compression curves was 200-230 mL mol-1 but four times as large when derived from the displacement of the compression curves with total protein concentration. This large discrepancy can be explained by the existence in the native tetramer population of a distribution of free energies of association with a dispersion from the mean of about 6 kcal mol-1. At 0 degree C and 1 bar ATP and ADP decreased the stability of the GAPDH tetramer by changes in free energy of association of +3.7 and +4.1 kcal mol-1, respectively. NAD and c-AMP stabilized it by -2.3 and -1.3 kcal mol-1. The variation in sign and magnitude of the ligand-induced changes in free energy of association observed in this case, and previously in hexokinase [Ruan, K., & Weber, G. (1988) Biochemistry 27, 3295], and the heterogeneity of the free energy of association of GAPDH, revealed as indicated above, lead to the conclusion that oligomeric aggregates exist in a variety of conformations that depend upon the protein concentration, temperature, pressure, and the presence of specific ligands. The multiplicity of species revealed by the energetics raises questions about the significance of the structures of oligomeric proteins determined by X-ray crystallography.

Adenosine Diphosphate↗

PubMed1986

Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes.

Glyceraldehydephosphate dehydrogenase purified from rabbit skeletal muscle is auto-phosphorylated with MgATP. Half-maximal phosphorylation is achieved around 0.3 mM. The phosphorylation is Ca2+ independent. The phosphoenzyme complex is labile in alkaline conditions and stable in moderately acid media. The complex is readily hydrolyzed by 0.1 M neutral hydroxylamine, indicating the complex formed is a high-energy acyl phosphate. The phosphorylation is reduced by nicotinamide adenine dinucleotides, reduced form (NADH), glyceraldehyde 3-phosphate, and nicotinamide adenine dinucleotide (NAD+). The enzyme is also dephosphorylated by these metabolites although to a lesser extent by NAD+. Calsequestrin isolated from rabbit skeletal muscle inhibits the phosphorylation of the enzyme. The phosphoenzyme behaves as a kinase catalyzing the phosphorylation of proteins of Mr 80 000 and 72 000 found in the skeletal muscle terminal cisternae/triad preparation. This reaction is enhanced by NADH. The phosphate found in the protein substrate has been shown to be the same phosphate initially involved in the phosphorylation of glyceraldehydephosphate dehydrogenase.

Adenosine Triphosphate↗

PubMed1977

Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle.

Methods for standardized determination of phosphofructokinase (PFK), glyceraldehydephosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) activities in nanogram samples of microdissected single fibres of rabbit psoas and soleus muscle are described. Fast and slow fibres in soleus muscle show lower absolute activities of these enzymes than the respective fibre types in psoas muscle. Slow fibres represent a more uniform population in the two muscles according to absolute and relative activities of the enzymes investigated. Slow fibres are characterized by high activities of MDH and relatively low activities of glycolytic enzymes. Fast fibres in the soleus muscle represent a population with high activities of MDH and glycolytic enzymes. Fast fibres in psoas muscle represent a heterogeneous population with high activities of glycolytic enzymes and extremely variable activity of MDH. More than 10-fold differences exist in the MDH activities of the extreme types of this fibre population. Differences in the activity levels of MDH in single fast type fibres but also in the activities of glycolytic enzymes between fast and slow fibres are greater than those reported between extreme white and red rabbit muscles.

Animals↗

PubMed1997

Effect of mebendazole and praziquantel on glucosephosphate isomerase and glyceraldehydephosphate dehydrogenase in Echinococcus granulosus cyst wall harbored in mice.

AIM: To study effects of antihydatid drugs on glucosephosphate isomerase (GPI) and glyceraldehydephosphate dehydrogenase (GAPDH) in Echinococcus granulosus cyst wall. METHODS: Mice infected with the parasite for 8-10 months were treated i.g. with mebendazole (Meb) or praziquantel (Pra). The activities of GPI and GAPDH in the cysts were measured by the formation of NADH or NADPH. RESULTS: GPI activity in the cyst wall was 197 +/- 103 U, while that of GAPDH was 25 +/- 13 U. When infected mice were treated i.g. with Meb 25-50 mg.kg-1.d-1 for 7-14 d, no apparent effect on the GAPDH activity in the cyst was found. In mice treated i.g. with praziquantel (Pra) 500 mg.kg-1.d-1 for 14 d, the GAPDH activity in the cyst wall was inhibited by 26.5%. As to GPI activity only the group treated i.g. with Meb 25 mg.kg-1.d-1 for 14 d showed 33.2% inhibition of the enzyme in the collapsed cyst wall. CONCLUSION: GPI and GAPDH are not the major targets attacked by the antihydatid drug.

Animals↗

PubMed1973