SEARCH · Search PubMed

Results for “PHOSPHOGLUCOMUTASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,495 records · Page 83Linked to original sources

PubMed1975

A specific enzyme for glucose 1,6-bisphosphate synthesis.

The reaction: glycerate-1,3-P2 PLUS GLUCOSE-1-P YIELDS TO GLUCOSE-1,6-P2 plus glycerate-P is catalyzed by a distinct enzyme of mouse brain. A divalent metal requirement was shown when the enzyme was treated with imidazole and EDTA. Mg2+, Mn2+, Ca2+, Zn2+, Ni2+, Co2+, and Cd2+ were quite effective cofactors. The enzyme, in better than 50 percent yield, has been purified away from 99 percent of the phosphoglucomutase, phosphoglycrate mutase, and phosphofructokinase. Acetyl-P, ATP, enolpyruvate-P, creatine-P, and fructose-1,6-P2 are not phosphoryl donors. Glucose-6-P and mannose-1-P are good alternate acceptors. Mannose-6-P, galactose-Ps, and fructose-Ps have little or no acceptor activity. Strong inhibition was found with fructose-1,6-P2, glycerate-2,3-P2, enolpyruvate-P, and acetyl CoA. From the amount of activity and the kinetic constants of the purified enzyme it seems likely that this enzyme is responsible for the glucose-1,6-P2 synthesis of brain.

Acetyl Coenzyme A↗

PubMed1975

In vivo hepatic and intestinal toxicity of sodium cyanate in rats: cyanate-induced alterations in hepatic glycogen metabolism.

To determine the hepatic and intestinal toxicity of sodium cyanate, this compound was administered to rats by orogastric tube (PO) or intraperitoneal injection (IP). At low dosage (50 mg. per kilogram per day PO for 8 weeks), the animals showed no clinical effects other than mild lethargy. They had normal intestinal absorption studies, but demonstrated decreased liver G6PD activity and a slight increase in hepatic glycogen. At higher dose levels (200 mg. per kilogram per day PO for 10 days, 400 mg. per kilogram per day PO for 3 days, and 100 mg. per kilogram per day IP for 10 days), the animals became very lethargic and developed hind-limb paralysis; many animals died during the period of dosing. The severity and rate of onset of symptoms increased proportionally with the dose level. Liver sections from rats receiving these higher doses showed striking increases in glycogen deposition. Activities of hepatic enzymes involved in glycogen synthesis and degradation were measured in rats receiving 200 mg. per kilogram per day PO or 100 mg. per kilogram per day IP. Significant decreases were noted in the activities of glucose-6-phosphatase and G6PD in PO-dosed rats. The activities of phosphorylase, UDPG-pyrophosphorylase, glycogen synthetase, phosphoglucomutase, and debrancher did not differ from control rats. In IP-dosed rats, significant decreases were observed in the activities of glucose-6-phosphatase, G6PD, phosphorylase, and UDPG-pyrophosphorylase, but not in the other glycogen-related enzymes. Our data suggest that sodium cyanate affects several enzymes of hepatic glycogen metabolism but that the enzymes vary in their susceptibility (glucose-6-phosphatase and G6PD greater than phosphorylase and UDPG pyrophosphorylase.

Animals↗

PubMed1989

Effect of dietary fiber from banana (Musa paradisiaca) on metabolism of carbohydrates in rats fed cholesterol free diet.

Effect of feeding isolated dietary fiber from M. paradisiaca on the metabolism of carbohydrates in the liver has been studied. Fiber fed rats showed significantly lower levels of fasting blood glucose and higher concentration of liver glycogen. Activity of glycogen phosphorylase, glucose-1-phosphate, uridyl transferase and glycogen synthase was significantly higher while phosphoglucomutase activity showed lower activity. Activity of some glycolytic enzymes, viz. hexokinase and pyruvic kinase was lower. Glucose-6-phosphatase showed higher activity while fructose 1-6 diphosphatase activity was not affected. Glucose-6-phosphate dehydrogenase on the other hand showed higher activity. The changes in these enzyme activities have been attributed due to the effect of higher concentration of bile acids produced in the liver as a result of feeding fiber. Evidence for this has been obtained by studying the in vitro effect of cholic acid and chenodeoxy cholic acid.

Animals↗

PubMed1989

Dispermic chimera associated with dysgerminoma.

A 12-year-old female patient (Miss E.Y.) suffering from abdominal tumor was proved to be a dispermic or generalized chimera. Ninety-two percent of her red cells were group A1, the first locus of phosphoglucomutase (PGM1) 1A, 6-phosphogluconate dehydrogenase (PGD) AC and 8% of them were group B, PGM1 1A-2A, PGD A. Ninety cells out of one hundred and ten cultured lymphocytes were normal 46 XY and 20 cells were normal 46 XX. She secreted B and H substances at normal secretor range and a small amount of A substance in her saliva. The A-transferase level found in her serum was about 40% of those of group A1 individuals. The B-transferase level was in the normal range. Her hairs had B antigen and PGM1 phenotype of their root cells was 1A-2A. The cells of hair root were X chromatin-positive and Y body-negative. Her nails had lesser A antigen and potent B antigen. Major epithelial cells (approximately 75%) of her buccal mucosa expressed B antigen and minor cells expressed A antigen. The proportion of the X chromatin-positive buccal cells (15%) was lower than those in normal females (20-25%) and that of Y body-positive buccal cells (10%) was higher than those in normal females (0-3%). The surgically resected abdominal tumor was her right uterine adnexa with malignant transformation, the histological diagnosis of which was dysgerminoma. The tumor cell nest and the epithelial cells of ductal structure expressed A antigen, whereas the endothelial cells of blood vessels expressed B antigen. These findings showed that the proband's body cells arose from the two cell lines, one carrying A1 gene had normal 46 XY male karyotype and another carrying B gene had normal 46 XX female karyotype, and suggested that her right gonad which was contributed by the former cell line had a malignancy in the presence of Y chromosome.

ABO Blood-Group System↗

PubMed1989

[Genetic markers and susceptibility to hypertension].

Genetic markers Hp, Gc, EstD and phosphoglucomutase (PGM) were studied in patients with essential hypertension (EH). The authors proved relationship between GcI-I-genotype and predisposition to EH. Heterozygote type 1-2 of the Gc-system was more resistant to the disease. The authors conclude that genetics markers may make the basis for studying the EH etiology and determining its more etiologically similar forms.

Disease Susceptibility↗

PubMed1989

Synthesis and properties of 5-azido-UDP-glucose. Development of photoaffinity probes for nucleotide diphosphate sugar binding sites.

A new active site directed photoaffinity probe, which is a model compound for studying nucleotide diphosphate sugar binding proteins, has been synthesized by coupling 5-azido-UTP and [32P]Glc-1-P using yeast UDP-glucose pyrophosphorylase to produce [beta-32P]5-azidouridine 5'-diphosphoglucose (5N3UDP-Glc). This probe has photochemical properties similar to that of 5-azidoUTP (Evans, R. K., and Haley, B. E. (1987) Biochemistry 26, 269-276). The efficacy of 5N3UDP-Glc as an active site directed probe was demonstrated using yeast UDP-Glc pyrophosphorylase. Saturation effects of photoinsertion were observed with an apparent Kd of 51 microM and the natural substrate, UDP-Glc, prevented photoinsertion of [beta-32P]5N3UDP-Glc with an apparent Kd of 87 microM. Prevention of photoinsertion was also seen with UTP and pyrophosphate with apparent Kd values less than 200 microM. UMP, UDP, ATP, and GTP were much less effective competitors. Selective photoinsertion was observed with several partially purified enzymes including UDP-Glc dehydrogenase, UDP-Gal-4-epimerase, Gal-1-P uridyltransferase, and phosphorylase a. The absence of nonselective photoinsertion into bulk proteins was demonstrated with crude homogenates of rabbit liver as well as with several UDP-Glc binding proteins. Of the six purified enzymes tested, only phosphoglucomutase has been shown to incorporate radiolabel from the photoprobe in the absence of UV irradiation. These results and a discussion of the utility of 5N3UDP-Glc for detecting UDP-Glc binding proteins and isolating active site peptides are presented.

Affinity Labels↗

PubMed1989

[Biochemical analysis using biopsied muscle in 72 patients with metabolic myopathies].

Biochemical analysis using biopsied muscle specimens was performed on 72 cases who had symptoms suggesting metabolic myopathies. Sixteen out of 72 cases (22%) were diagnosed as having chemically confirmed metabolic defects. Of these 16 cases, 9 had defects in the glycolytic pathway (glycogen storage disease type II; 3 cases, type III; 1 case, type V; 3 cases, phosphoglycerate kinase deficiency; 1 case, phosphoglucomutase deficiency; 1 case) and 7 cases in mitochondrial metabolism (complex IV deficiency; 4 cases, carnitine deficiency; 3 cases). Among 14 cases who were strongly suspected as having a defect in the glycolytic pathway because of abnormal ischemic forearm test, 6 (43%) showed biochemically proved glycolytic defects. These data suggest that care should be taken when evaluating the results of ischemic forearm test. In addition, we should carefully interpret the muscle histochemistry, because histochemical stains including PAS might be fairly normal in the defects with second step glycolytic pathway.

Adolescent↗

PubMed1987

Examination of the mechanism of sucrose synthetase by positional isotope exchange.

The mechanism of the sucrose synthetase reaction has been probed by the technique of positional isotope exchange. [beta-18O2, alpha beta-18O]UDP-Glc has been synthesized starting from oxygen-18-labeled phosphate and the combined activities of carbamate kinase, hexokinase, phosphoglucomutase, and uridine diphosphoglucose pyrophosphorylase. The oxygen-18 at the alpha beta-bridge position of the labeled UDP-Glc has been shown to cause a 0.014 ppm upfield chemical shift in the 31P NMR spectrum of both the alpha- and beta-phosphorus atoms in UDP-Glc relative to the unlabeled compound. The chemical shift induced by each of the beta-nonbridge oxygen-18 atoms was 0.030 ppm. Incubation of [beta-18O2, alpha beta-18O]UDP-Glc with sucrose synthetase in the presence and absence of 2,5-anhydromannitol did not result in any significant exchange of an oxygen-18 from the beta-nonbridge position to the anomeric oxygen of the glucose moiety. It can thus be concluded that either sucrose synthetase does not catalyze the cleavage of the scissile carbon-oxygen bond of UDP-Glc in the absence of fructose or, alternatively, the beta-phosphoryl group of the newly formed UDP is rotationally immobilized.

Glucosyltransferases↗

PubMed1986

Glucose 6-phosphate regulates Ca2+ steady state in endoplasmic reticulum of islets. A possible link in glucose-induced insulin secretion.

Glucose stimulation of islets is coupled with the rapid intracellular release of myo-inositol 1,4,5-trisphosphate (IP3) and arachidonic acid which in turn mobilize Ca2+ stored in the endoplasmic reticulum (ER). The metabolism of glucose is required for insulin secretion although the link between glucose metabolism and the cellular events resulting in insulin release is unknown. In digitonin-permeabilized islets, glucose 6-phosphate (0.5-4 mM) increased significantly the ATP-dependent Ca2+ content of the ER at a free Ca2+ concentration of 1 microM. At 0.2 microM free Ca2+, glucose 6-phosphate (2-10 mM) had a smaller effect. Glucose, phosphate, mannose 6-phosphate, and fructose 1,6-diphosphate had no effect on the ATP-dependent Ca2+ content of the ER. Glucose 1-phosphate and fructose 6-phosphate also increased ATP-dependent Ca2+ content of the ER, presumably due to conversion to glucose 6-phosphate by islet phosphoglucomutase and phosphoglucoisomerase, respectively. The glucose 6-phosphate increase in the ATP-dependent Ca2+ content of the ER was shown to be mediated by glucose 6-phosphatase localized to the ER. Both arachidonic acid (10 microM) and the Ca2+ ionophore A23187 (2 microM) mobilized Ca2+ stored in the ER by glucose 6-phosphate. However, IP3-induced (10 microM) Ca2+ release from the ER was abolished in the presence of glucose 6-phosphate (0.5-10 mM). We propose that glucose 6-phosphate could provide a regulatory link between glucose metabolism and intracellular Ca2+ regulation by augmenting Ca2+ sequestered in the ER as well as attenuating IP3-induced Ca2+ release. Thus, glucose 6-phosphate would serve as an "off" signal leading to a decrease in intracellular Ca2+ when both the free Ca2+ and glucose 6-phosphate concentrations have increased following glucose stimulus.

Animals↗

PubMed1987

The cellular retinol binding protein II gene. Sequence analysis of the rat gene, chromosomal localization in mice and humans, and documentation of its close linkage to the cellular retinol binding protein gene.

Cellular retinol binding protein II (CRBP II) is an abundant, 134-residue protein present in the small intestinal epithelium. It is thought to participate in the uptake and/or intracellular metabolism of vitamin A. We have isolated and sequenced the rat CRBP II gene. Its four exons span 0.65 kilobases and are interrupted by three introns with an aggregate length of 19.5 kilobases. Southern blot hybridization analysis indicated that this gene is highly conserved in rats, mice, and humans. CRBP II belongs to a protein family that contains eight known members. Computer-assisted comparative sequence analyses indicated that a region of internal homology spans its first two exons and that oligopeptide domains specified by these first two exons exhibit significant homology to all other family members as well as to a portion of the all-trans-retinol binding domain that has previously been defined in serum retinol binding protein. The CRBP II gene was mapped in mice using recombinant inbred strains and restriction fragment length polymorphisms. It is located on chromosome 9 within 5.3 centimorgans of the phosphoglucomutase-3 locus and is closely linked (within 3.0 centimorgans) to the gene specifying a highly homologous intracellular retinol binding protein known as CRBP. Mouse-human somatic cell hybrids were used to determine that both the CRBP and CRBP II genes are located on human chromosome 3.

Amino Acid Sequence↗

PubMedDate not supplied

Red cell enzyme polymorphisms in Papua New Guinea Eastern Highlands.

Ten red cell enzyme polymorphisms, malic dehydrogenase (MDH1), adenylate kinase (AK), phosphohexose isomerase (PHI), adenosine deaminase (ADA), esterase D (ESD), glutamic pyruvic transaminase (GPT), acid phosphatase (ACP1), phosphoglucomutase 1 and 2 (PGM1, PGM2), phosphogluconate dehydrogenase (PGD) were investigated in the Baruya tribe and several Anga tribes living high in the Wonenara and Marawaka valleys in Papua New Guinea Eastern Highlands (6.5S, 145.5E). Also a non-Anga tribe, the Aziana or Kenaze, was sampled. Variants were observed in ADA, PGM1 and PGM2. AK and PHI were monomorphic, all subjects being AK 1 and PHI 1; MDH1 was also monomorphic in Anga while variants were observed in Aziana. This latter tribe differed markedly in each system from the Anga peoples.

Alleles↗

PubMedDate not supplied

Quantitation of electrophoretic eluted proteins.

Quantitation of stained, electroeluted proteins by the classical Lowry and Bradford protein assay is not possible because of some different interferences. In particular we have found that the substance interfering in the Lowry method cannot be removed by trichloroacetic acid precipitation nor can be compensated for by the appropriate blank. Interferences in the Bradford protein assay are due to detergents and pH of the protein buffer as well as to Coomassie brilliant blue R250 electroeluted with the protein sample. However, while these interferences can be compensated for by appropriate blank and standard curves, others (probably due to acrylamide fines) cannot be corrected. All these problems can be overcome by concentration and dialysis of electroeluted samples which permit the removal of interfering substances and the use of Bradford and Lowry protein assay in the 1-20 micrograms range, respectively. Successful applications are described for electroeluted bovine serum albumin, human hexokinase and phosphoglucomutase.

Animals↗

PubMed1988

Genetic differentiation and biochemical polymorphism among trichomonads.

Isoenzyme electrophoresis was used to study levels of genetic differentiation among strains and clones of Trichomonas gallinae, Trichomonas vaginalis, Tritrichomonas foetus, Tetratrichomonas gallinarum, and Pentatrichomonas hominis. Strain variation was found within T. gallinae, T. vaginalis, and T. foetus, however, levels of enzyme polymorphism were greater in T. gallinae than in T. vaginalis or T. foetus. Isoenzyme genotypes were not a stable property of T. gallinae clones cultivated in vitro. Retrospective studies of T. gallinae SG and JB6 clones revealed that mutation occurred during in vitro cultivation. Heterozygotes of hexokinase-1 and phosphoglucomutase displayed 2 allomorphs in equal dosage, indicating that trichomonads are diploid for these protein loci. Phenetic clustering of the biochemical data suggests that levels of genetic divergence among the species studied are extensive.

Animals↗

PubMed1987

Regional assignment of human alcohol dehydrogenase (ADH) gene to 4pter----4q21.

The hybrid clone FD1 constructed by fusion of Chinese hamster cell line Wg3-h with human lymphocyte was irradiated with X-ray. Fourteen survival clones were isolated and 3 of them, F5B, F52B, F61A were analyzed in detail by cytogenetic and biochemical methods. The results of chromosome G-banding followed by Giemsa-11 differential staining show that there exists a deleted human chromosome 4 in all of the three hybrids. This deletion of human chromosome 4 in F61A is 4pter----4q21. The results of isozyme analysis of phosphoglucomutase-2 (PGM2) which is located on 4p14----4q21 confirm our cytogenetic conclusion. We used polyacrylamide gel electrophoresis to study the alcohol dehydrogenase (ADH) in human lymphocyte, Wg3-h and hybrid clones. Their electrophoretic pattern showed that human ADH isozyme did express, in the peripheral blood lymphocyte, hybrids F5B, F52B, F61A and FD1. According to these results, we suggest that one of the Class I ADH structural genes is located on the human chromosome 4pter----4q21. Recently, McKusick reported that Class I ADH gene cluster had been assigned to chromosome 4q21----4qter. Considering this fact, we suggest that Class I ADH gene might be assigned to chromosome 4q21 or on its vicinity.

Alcohol Dehydrogenase↗

PubMed1986

Interactions of immobilized and free triazine dyes with glucose-6-phosphate dehydrogenase from yeast.

Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) prepared from baker's yeast binds to immobilized Cibacron Blue F3G-A and Procion Red HE-3B. In this paper the two dyes are compared with respect to their use in the purification of this enzyme. Cibacron Blue chromatography was found useful at an early stage of purification for the removal of contaminating hexokinase, phosphoglucose isomerase and phosphoglucomutase. With Procion Red HE-3B Sepharose the NADP dependent enzymes phosphogluconate dehydrogenase and glutathione reductase are separable from glucose-6-phosphate dehydrogenase. Unlike Cibacron Blue gel chromatography, the enzyme can be specifically eluted from Procion Red HE-3B Sepharose by a NADP gradient. Other monochlorotriazine dyes like Xirone Brillant Red BHD, 4BHD, 6BHD and GHD and the dichlorotriazine dye Procion Brown MX-5BR immobilized to Sepharose have only little binding affinity to glucose-6-phosphate dehydrogenase. The binding behaviour of different immobilized triazine dyes for pre-purified and purified glucose-6-phosphate dehydrogenase is compared. In addition, the influence of the free dyes on the activity of glucose-6-phosphate dehydrogenase is studied. It is demonstrated that the results of kinetic and binding studies with the purified enzyme are not uncritically applicable for the selection of a dye as ligand for affinity chromatography during enzyme preparation.

Chromatography, Affinity↗

PubMed1986

The influence of fructose-1:6-bisphosphate on the release of glycolytic enzymes from cellular structure.

In order to provide information on the relative binding characteristics of glycolytic enzymes, the effect of fructose-1,6-bisphosphate (FBP) on the release of glycolytic enzymes from cultured pig kidney cells treated with digitonin has been studied. In the absence of FBP, a differential release of these enzymes was observed, with the order of retention being aldolase greater than glyceraldehyde-3-phosphate dehydrogenase greater than glucosephosphate isomerase, triosephosphate isomerase, phosphoglycerokinase, phosphoglucomutase, lactate dehydrogenase, enolase, pyruvate kinase and phosphofructokinase. In the presence of fructose-1,6-bisphosphate, the release of aldolase was considerably enhanced, whereas the release of phosphofructokinase and pyruvate kinase was decreased by this metabolite. No significant alterations in the rate of release of the other enzymes was caused by FBP. These data have been discussed in relation to their contribution to the knowledge of the degree of association and order of binding between glycolytic enzymes and the cytoplasmic matrix.

Animals↗

PubMed1985

Twenty-seven protein polymorphisms by two-dimensional electrophoresis of serum, erythrocytes, and fibroblasts in two pedigrees.

Twenty-seven independent polymorphic loci were detected by two-dimensional electrophoresis (2DE) of serum, erythrocytes, and fibroblasts in two large families and analyzed for linkage to classical genetic markers. We detected seven serum, four erythrocyte, and 17 fibroblast protein loci that exhibited charge variation in these two families and in a sample of unrelated individuals. The genetic basis of protein variants was confirmed by quantitative gene-dosage dependence and by conformance to Mendelian transmission in the two families, except for four rare variants for which transmission analysis was not possible. Linkage analysis demonstrated that each of the variants represent products of independent loci, with the exception of erythrocyte locus (RBC4), which we also detected in fibroblasts (NC27). Two allozyme polymorphisms, glyoxalase-1 (GLO1) and phosphoglucomutase-3 (PGM3) were specifically identified here based on genotypic concordance and molecular mass. Unknown fibroblast protein (NC22) may be linked to apolipoprotein E (lod score = 2.8 at theta m = theta f = 0), while a serum protein locus (SER1) may be linked to alpha-haptoglobin (lod score = 2.54 at theta m = .20, theta f = .01). Six of seven polymorphic serum loci were previously located on two-dimensional gels: alpha-1 antitrypsin (PI), Gc-globulin (GC), alpha-2 HS glycoprotein (HSGA), alpha-haptoglobin (HP), and two apolipoproteins (APOE and APOA4). Six of 17 polymorphisms detected in fibroblasts were positionally identical to polymorphic loci seen in lymphocytes. These studies indicate a minimum level of average protein charge heterozygosity of approximately 2.2% for the most predominant human cellular proteins and of 5.6% for the most predominant proteins of serum.

Alleles↗

PubMed1966

Myoglobinuria and skeletal muscle phosphorylase deficiency: report of a case of McArdle's disease.

Investigation of a patient complaining of exercise-induced dark urine, pain, stiffness and tenderness of skeletal muscle revealed findings characteristic of McArdle's disease. The dark urine was attributable to the excretion of myoglobin, and an ischemic exercise test failed to demonstrate the usual rise and fall in blood lactate and pyruvate. Enzyme assays of skeletal muscle showed an absence of phosphorylase, a slight increase in phosphorylase b kinase and a slight decrease in phosphoglucomutase. Chemical and histochemical analyses demonstrated an increase in the skeletal muscle glycogen content and an enlargement of the muscle cells. No abnormality of liver glycogen metabolism was found. In the absence of specific therapy, an effective and practical form of treatment is reduction of exercise below the threshold of symptoms.

Adult↗