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Results for “Diphosphoglyceric Acids”

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At least 19 recordsLinked to original sources
PubMed1978

Synthesis and characterization of N-(2,4-diphosphobenzyl)-1-amino-5-naphthalenesulfonic acid, a new fluorescent analogue of diphosphoglyceric acid.

The synthesis of N-(2,4-diphosphobenzyl)-1-amino-5-naphthalenesulfonic acid (DIPANS) is described. It entails the synthesis of 2,4-diphosphobenzaldehyde from the action of POCl3 on 2,4-dihydroxybenzaldehyde. This is followed by coupling of the 2,4-diphosphobenzaldehyde to 1-amino-5-naphthalenesulfonic acid. Subsequent reduction with NaBH4 yields the desired product. The DIPANS exhibits an excitation maximum at 337 nm and a fluorescence emission maximum at 504 nm. This dye is quantitatively displaced by inositol hexaphosphate and is an effective analogus of diphosphoglyceric acid (DPG), possessing a KD at pH 7.0 in 0.05 M [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)methane (bis-Tris) plus 0.1 M chloride of 6.88 microgram, with 1.0 molecule bound/hemoglobin tetramer. Like DPG its binding to deoxyhemoglobin decreases with increasing pH; in the presence of 0.1 M chloride it binds 0.031 times as tightly to CO hemoglobin and it yields a value for free energy coupling of 2.0 kcal/mol. The presence of 1 mM DIPANS decreases the affinity of hemoglobin for oxygen in the absence of salt from p1/2 of 0.8 mm Hg to 12.4 mm Hg. Using DPG as a competitor of DIPANS binding, a dissociation constant of 11.4 micrometer was calculated for DPG binding to deoxy-Hb at pH 7.0 in the presence of 0.05 M bis-Tris and 0.1 M chloride.

Binding, Competitive↗
PubMed1970

Mechanism of action of thyroid hormones on erythrocyte 2,3-diphosphoglyceric acid synthesis.

Normal erythrocytes, when incubated with thyroid hormone, were found to have increased levels of 2,3-diphosphoglyceric acid. In addition, a partially purified enzyme preparation, when incubated with either a 1,3-diphosphoglyceric acid generating system or 1,3-diphosphoglyceric acid directly, showed increased levels of 2,3-diphosphoglyceric acid when exposed to thyroid hormone. The hormonal effect was biphasic and was witnessed after 5 min of incubation. Substitution on the 3 and 5 positions of the basic thyronine molecule was essential for hormonal effect. It appears that thyroid hormone acts by directly stimulating the diphosphoglycerate mutase enzyme. The hormonal effect on 2,3-DPG synthesis may offer a biochemical explanation for the shift in the oxyhemoglobin dissociation curve observed in thyroid disorders.

Adenosine Triphosphate↗
PubMed1984

Modulation of 3-hydroxy-3-methyl glutaryl CoA reductase by 2,3-diphosphoglyceric acid.

Rat liver microsomal 3-hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase was activated by 50% at a concentration of 0.4 mM 2,3-diphosphoglyceric acid (DPG) and by 11-fold at 10 mM DPG. DPG also prevented the inactivation of HMG-CoA reductase by ATP and Mg++. Rat liver microsomal HMG-CoA reductase prepared in the presence of 1 mM DPG was significantly more active than when prepared in the absence of DPG. Activation of the enzyme by DPG and protection of the enzyme against inhibition by ATP and Mg++ by DPG were also observed with solubilized HMG-CoA reductase.

2,3-Diphosphoglycerate↗
PubMed1994

2,3-diphosphoglyceric acid blocks long-term potentiation of excitatory postsynaptic currents in hippocampal CA1 neurons of the rat.

The dependence of long-term potentiation on an intact inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] metabolism was investigated with the whole-cell voltage-clamp method in the CA1 region of hippocampal slices. The intracellular application of 2,3-diphosphoglyceric acid (1 mM), an inhibitor of the Ins(1,4,5)P3 5-phosphatase and of Ins(1,4,5)P3 3-kinase eliminated the potentiation of postsynaptic currents in pyramidal cells 30 min after paired pre- and postsynaptic activation. These data suggest a possible role of postsynaptic inositol 1,4-bisphosphate and/or inositol 1,3,4,5-tetra-kisphosphate in synaptic plasticity.

2,3-Diphosphoglycerate↗
PubMed1992

Influence of the cryoprotective agents glycerol and hydroxyethyl starch on red blood cell ATP and 2,3-diphosphoglyceric acid levels.

Because hydroxyethyl starch (HAES) is used for volume replacement therapy and as a cryoprotectant for frozen red blood cells (RBCs), this compound, in contrast to glycerol, does not require labor-intensive removal from thawed cells prior to transfusion. We here report the effect of both glycerol and HAES on the RBC organic phosphates ATP and 2,3-diphosphoglyceric acid (2,3-DPG). The CPD-A1-stabilized RBCs of 20 healthy donors (3 females, 17 males) were separately frozen in either 40% glycerol or 6% HAES, of molecular weight 200,000. ATP and 2,3-DPG concentrations were determined in CPD-A1 RBCs before addition of cryoprotectant and in cryopreserved thawed RBCs after 24 h storage at -80 degrees C (glycerol) and -196 degrees C (HAES). It appears that HAES, but not glycerol, significantly reduces ATP concentrations whereas both lead to a reduction of 2,3-DPG concentrations; this reduction was more pronounced with glycerol than with HAES. Experiments with the blood of 6 donors demonstrated that HAES affects autohemolysis by 16%, in contrast to glycerol, after which cryoprotectant autohemolysis was affected by 3.1% only. RBC recoveries were comparable using glycerol or HAES as cryoprotectants. A distinct pattern of reduction of 2,3-DPG levels by glycerol and less by HAES, and of ATP levels by HAES but not by glycerol, emerges. Our findings may be of importance if HAES is to be introduced as a convenient cryoprotectant.

2,3-Diphosphoglycerate↗
PubMed1982

Canine cyclic hematopoiesis: blood gas and 2,3-diphosphoglyceric acid studies.

Cyclic hematopoiesis in gray Collies was first described in 1967. These dogs are anemic in comparison with the healthy littermates, and their erythropoiesis is abnormal. Although the basic disorder appears to be an as yet unidentified abnormality of hematopoietic progenitor cells, an inherent difference in responses to blood gas control mechanisms remains as a possible cause. In a study of these mechanisms in dogs with cyclic hematopoiesis, the P50 and 2,3-diphosphoglyceric acid concentrations were increased. Differences in pH, PCO2, PO2, and oxygen saturation were not observed.

2,3-Diphosphoglycerate↗
PubMed1989

Changes in blood viscosity following nifedipine administration and its relation to the contents of adenosine triphosphate and 2,3-diphosphoglyceric acid in red blood cells in patients with angina pectoris.

The effect of oral administration of nifedipine (Adalat) on whole blood viscosity in patients with angina pectoris was investigated. Whole blood viscosity at a low shear rate of 37.5 s-1 was significantly reduced from 7.90 +/- 0.18 cP to 7.30 +/- 0.27 cP (1 cP = 1 mPa x s) after nifedipine administration (p less than 0.01), though the value at the high shear rate of 375 s-1, Casson yield stress value and Casson viscosity hardly decreased. Content of adenosine triphosphate (ATP) and 2,3-diphosphoglyceric acid (2,3-DPG) in the erythrocytes affecting blood viscosity, especially low shear rate viscosity, showed little change, and the hematocrit value was little varied either. Nifedipine, a Ca antagonist, has been known to inhibit Ca entry into the cells. These findings suggest that nifedipine reduces whole blood viscosity, especially low shear rate value, due to inhibition of Ca entry into the red blood cells, without increasing metabolic changes of ATP or 2,3-DPG in the erythrocytes, though measurement of Ca content in erythrocyte was unsolved.

2,3-Diphosphoglycerate↗
PubMed1982

Kinetics of Phosphorylation of eIF-2 by the hemin-controlled repressor and casein kinase II. Inhibition by hemin and 2,3-diphosphoglyceric acid.

The kinetics of phosphorylation of eukaryotic initiation factor 2 (eIF-2) by two cyclic nucleotide-independent protein kinases from rabbit reticulocytes have been studied. The hemin-controlled repressor (HCR) and casein kinase II phosphorylate the alpha and beta subunits of eIF-2, respectively. The apparent Km for eIF-2 with HCR and casein kinase II was determined to be in the range of 0.5-1.0 microM. Using fully dephosphorylated eIF-2, it was possible to show that the phosphorylation state of the beta subunit did not affect the apparent Km of either HCR or casein kinase II for eIF-2. The effects of two inhibitory compounds, hemin and 2,3-diphosphoglyceric acid (2,3-DPG), were studied also. Hemin acted as a noncompetitive inhibitor of HCR with respect to eIF-2 with an apparent Ki of 3 microM, while inhibition of casein kinase II by 2,3-DPG was competitive with respect to eIF-2. The apparent inhibitory constant was determined to be 1 mM, a concentration within the physiological range of 2,3-DPG in red blood cells. From the kinetic values obtained with hemin and 2,3-DPG, it appears that these compounds could directly regulate the respective protein kinases in vivo.

2,3-Diphosphoglycerate↗
PubMed1986

Red blood cell 2,3-diphosphoglyceric acid following ethanol consumption in man.

The red blood cell 2,3-diphosphoglycerate (DPG) concentration is reported in 33 ethanol abusers, 16 healthy ethanol users and 14 non-users. The results demonstrate an ethanol-associated increase in DPG content which returns to normal exponentially in the week following alcohol withdrawal. As well as implying a significant degree of hypoxia in association with quite moderate drinking, the fact that ethanol is not catabolized in red cells indicates that this effect is transmitted there, and hence to the rest of the organism, by some other agent. Carbon dioxide in subnormal quantities has the necessary characteristics.

Alcohol Drinking↗
PubMed1981

Effects of 2,3-diphosphoglyceric acid on the human erythrocyte membrane phosphorylation system.

The effect of 2,3-diphosphoglycerate (2,3-P2-glycerate) on the phosphorylation of spectrin in solution by purified membrane cyclic AMP-independent protein kinase and in membrane preparations by the endogenous kinase was investigated. 2,3-P2-Glycerate inhibited spectrin phosphorylation both in solution and in the intact membrane. Kinetic analyses showed that 2,3-P2-glycerate had no effect on the Km for ATP but appeared to lower the Vmax of the reaction. When the effect of 2,3-P2-glycerate was examined in the presence of varying concentrations of spectrin, competitive inhibition kinetics were obtained. Interestingly, low concentrations of 2,3-P2-glycerate were found to effect the release of the membrane kinase from erythrocyte membranes. This release reaction may be related to the ability of 2,3-P2-glycerate to interfere with the interaction between the kinase and spectrin. The data suggest the possibility that the kinase may be bound to spectrin in the erythrocyte membrane. 2,3-P2-glycerate also caused the solubilization of 3-phosphoglyceraldehyde dehydrogenase, but not of cyclic AMP-dependent protein kinase. Taken together, our data indicate that 2,3-P2-glycerate may have a regulatory role in membrane protein phosphorylation and also may regulate the extent of association of the kinase with the membrane.

2,3-Diphosphoglycerate↗