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PubMed1990

[Enzyme activity of PGM1 in erythrocytes].

The enzyme activity of phosphoglucomutase (PGM) has been investigated in red cell haemolysates from 142 individuals and compared to the sub-type as determined by isoelectric focusing. The 10 phenotypes showed significant differences in PGM-activity which indicates that there is a correlation between the level of activity and the isolelectric point of homozygotes. No indication of silent alleles or alleles with reduced activity was found in this collective.

Erythrocytes↗
PubMed1980

An electrophoretic polymorphism that mimics a true genetic polymorphism in Triturus cristatus carnifex (Amiphibia, Urodela).

Phosphoglucomutase electrophoretic patterns have been studied in 60 tail homogenates of Triturus cristatus carnifex. Our results show that the same sample produces a different electrophoretic pattern with homogenate ageing; a new band of intermediate mobility appears, together with the one produced by the fresh preparation. The phenomenon can mimic a true genetic polymorphism when differently stored samples are analyzed.

Animals↗
PubMed1982

[Detection of hereditary enzyme characteristics in vaginal secretion].

Upon investigation of semen- and blood-free vaginal swabs using starch gel electrophoresis the Phosphoglucomutase type was clearly identified in about 40%. Using cellulose acetate membrane electrophoresis PGM could not be demonstrated. In all cases the results correspond with those obtained in blood. No relation was found between secretor type (determined in saliva) and PGM typing. In vaginal material the following could not be determined: Adenylatkinase (AK) using starch gel electrophoresis, Esterase D (EsD) using cellulose acetate membrane electrophoresis, and Glyoxalase I (GLO) using agarose gel thin-layer electrophoresis.

Adenylate Kinase↗
PubMed1979

Investigations of gestation-induced metabolic changes in the rat liver. I. Glycogen metabolism.

The activities of alpha-glucan-phosphorylase and phosphoglucomutase and the concentration of glycogen were measured in the liver of pregnant and non-pregnant rats. There were no significant differences between normal non-pregnant and pregnant animals nor was there any change of enzyme activities during pregnancy. Our results lend support to the idea that glycogen metabolism is not changed during normal pregnancy.

Animals↗
PubMed2005

Exopolysaccharide biosynthesis by Lactobacillus helveticus ATCC 15807.

Exopolysaccharide (EPS) production and the activities of the enzymes involved in sugar nucleotide biosynthesis in Lactobacillus helveticus ATCC 15807 under controlled pH conditions were investigated. Batch fermentations using lactose as energy source showed higher EPS synthesis by L. helveticus ATCC 15807 at pH 4.5 with respect to pH 6.2, the enzyme alpha-phosphoglucomutase (alpha-PGM) being correlated with both total and specific EPS production. When glucose was used as carbon source instead of lactose, the lower EPS synthesis obtained was linked to a decrease in alpha-PGM and galactose 1-phosphate-uridyltransferase (GalT) activities, the reduction of the latter being more pronounced. Higher EPS production by L. helveticus ATCC 15807 at the acidic constant pH of 4.5 requires that both alpha-PGM and GalT activities are high. These enzymes are needed to synthesize UDP-glucose and UDP-galactose for supplying the corresponding monomers for EPS biosynthesis. Although differences are observed in EPS production by this strain regarding the energy source (lactose or glucose), the monomeric composition of the polymers produced is independent of the carbohydrate used. The obtained results contribute to a better understanding of the physiological factors that affect EPS biosynthesis by lactobacilli, which could help in the correct handling of the fermentation parameters within the fermented dairy industry.

Culture Media↗
PubMed1996

Chromosome localization of the loci for PEPA, PEPB, PEPS, IDH1, GSR, MPI, PGM1, NP, SOD1, and ME1 in the common shrew (Sorex araneus).

This report extends the genetic map of the common shrew (Sorex araneus) by adding chromosome assignments for ten genes to the seven already mapped (Pack et al. 1995). A somatic cell hybrid panel was used for the mapping. The genes for peptidase A (PEPA) and isocitrate dehydrogenase-1 (IDH1) map to chromosome de; the genes for phosphoglucomutase-1 (PGM1), superoxide dismutase-1 (SOD1), and mannosephosphate isomerase (MPI) are located on chromosome af; the genes for nucleoside phosphorylase (NP) and glutathione reductase (GSR) are on chromosome ik; and the genes for peptidase S (PEPS), malic enzyme-1 (ME1), peptidase B (PEPB) are found on chromosomes jl, go, and mp respectively.

Aminopeptidases↗
PubMed1997

Isoenzymes of Eimeria from the domestic fowl: electrophoretic variants among species, strains and clones.

Electrophoretic variation of enzymes in five Eimeria spp. of the domestic fowl, including nine strains, ten single-sporocyst clones and two single-sporozoite clones of E. acervulina, three strains each of E. maxima and E. tenella, two strains of E. praecox and one strain of E. necatrix, were assayed using cellulose acetate electrophoresis. Ten enzymes [aldehyde oxidase (AO), alkaline phosphatase (ALP), amylase (AMY), fumarate hydratase (FUM), glucose-6-phosphate dehydrogenase (G6PDH), glucose phosphate isomerase (GPI), glutamate-oxaloacetate transferase (GOT), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH) and phosphoglucomutase (PGM)] were analyzed for their ability to distinguish between these species and strains. Enzymatic activity of G6PDH, GPI, IDH, MDH and PGM was detected in all the Eimeria spp. examined. Strains within each species were characterized by the same electrophoretic variant of G6PDH. Electrophoretic variants of GPI and PGM were the most valuable in the identification of inter- and intra-specific variation, particularly in the field strains of E. acervulina and E. tenella. These two enzymes were used to examine single-sporocyst and single-sporozoite clones derived from two strains of E. acervulina. The enzymes in E. maxima appeared to be conserved, showing no variation among strains with the five enzymes detected. Relative mobilities, calculated as described in this paper, were found to be consistent between different electrophoresis runs and may serve as a reference when this medium is used.

Animals↗
PubMed2000

Allozyme analysis of two polymorphic enzymes in a natural population of Lecithochirium musculus.

Genetic variability among 112 individuals of Lecithochirium musculus from Anguilla anguilla from northwestern Spain was examined using allozyme analysis. Starch-gel electrophoresis was used to investigate the genetic variation in two polymorphic enzymes, glucose phosphate isomerase (GPI) and phosphoglucomutase (PGM). The banding patterns obtained for GPI were consistent with a dimeric structure for this enzyme and with single-locus control. The inferred genotype frequencies did not significantly differ as compared with those predicted by the Hardy-Weinberg equation. Two PGM loci were detected (Pgm-1 and Pgm-2). Pgm-1 was polymorphic and showed a striking departure from Hardy-Weinberg predictions (total absence of heterozygotes for alleles in high frequencies), raising the possibility of the existence of two reproductively isolated populations. However, other reasons for this observation are discussed.

Anguilla↗
PubMed1983

A bioluminescent assay for glycogen phosphorylase in cultured cells.

A new method for the determination of glycogen phosphorylase (1,4 alpha-D-glucose:orthophosphate alpha-glucosyltransferase, EC 2.4.1.1) in cultured cells is described. The assay utilizes bacterial luciferase (EC 2.7) in a liquid scintillation spectrometer to measure NAD(P)H formed in a coupled enzyme reaction comprising glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and phosphoglucomutase (EC 2.7.5.1). This assay is highly sensitive, easily detecting as little as 10 microU phosphorylase, fast and simple to perform. With modifications this procedure can be extended to measure other glycogenolytic enzymes and intermediates.

Animals↗
PubMed1983

An enzymatic method for inosine 5'-monophosphate in the femtomole range.

A method for measuring inosine 5'-monophosphate (IMP) by enzymatic generation of NADPH is described. Procedures are given for direct fluorometric assay in the nanomole range and indirect measurement with amplification by enzymatic cycling in the pico- and femtomole ranges. The most sensitive procedure represents a nearly 50,000-fold increase in sensitivity over enzymatic methods now available. Specificity of the assay was greatly enhanced by the use of the antibiotic coformycin, a potent inhibitor of adenosine deaminase (EC 3.5.4.4). This enzyme was found to be a major contaminant of one of the necessary enzymes, phosphoglucomutase (EC 2.7.5.1). The use of the method is illustrated by measurements of IMP in single stimulated and control rat muscle fibers.

Adenosine Deaminase Inhibitors↗
PubMed1990

Enzymatic synthesis of UDP-GlcN by a two step hollow fiber enzyme reactor system.

UDP-GlcN was synthesized from GlcN and UTP by a two step hollow fiber enzyme reactor method. In step 1, GlcN was converted to GlcN 6-P and then to GlcN 1-P by hexokinase and phosphoglucomutase, respectively, and UTP was used as the phosphate donor. In step 2, GlcN 1-P was converted to UDP-GlcN by UDP glucose pyrophosphorylase. All the enzymes required for the synthesis of UDP-GlcN were enclosed in hollow fiber bundles which allow for the free diffusion of substrates and products across the membranes to and from the enzymes, allow for the reutilization of the enzymes, and simplify the isolation of the product, UDP-GlcN. We show that both UTP and GlcN 6-P are inhibitors of the yeast UDPG pyrophosphorylase and therefore their concentrations must be regulated to obtain maximum yields of UDP-GlcN. The UDP-GlcN produced can be N-acetylated with [14C]acetic anhydride to produce UDP-[14C]GlcNAc. This method can also be used to synthesize [32P]UDP-GlcN and [32P]UDP-GlcNAc from [alpha-32P]UTP and GlcN 1-P.

Acetylglucosamine↗
PubMed1994

Quantification and removal of glycogen phosphorylase and other enzymes associated with sarcoplasmic reticulum membrane preparations.

The enzymatic characterization of sarcoplasmic reticulum membrane fragments from rabbit skeletal muscle presented in this paper shows that glycogen phosphorylase, as well as other enzymes (e.g., creatine kinase, myokinase, phosphorylase kinase, glycosidase, AMP-deaminase, phosphoglucomutase) are associated with these membrane preparations. Amongst these enzymes, the highest activity associated with sarcoplasmic reticulum membranes is that of glycogen phosphorylase, which is mostly (at least 95%) in its b form (dephosphorylated form), since its activity in sarcoplasmic reticulum membranes is largely dependent upon AMP. A protocol is presented to quantify the amount of phosphorylase bound to sarcoplasmic reticulum membranes from fluorimetric measurements of the content of its coenzyme, pyridoxal 5'-phosphate. The content of phosphorylase ranged from 0.03 to 0.37 mg phosphorylase per mg of membrane protein, in sarcoplasmic reticulum membrane preparations made following several of the protocols most commonly used and also depending upon the length of the starvation period of the animal before killing. We also show that dilution of sarcoplasmic reticulum membranes to 0.1-0.2 mg protein per ml in a buffer containing 50 mM Tes-KOH (pH 7.4), 0.1 M KCl and 0.25 M sucrose removes at least 95% of glycogen phosphorylase from these membrane fragments, as well as other enzymes like myokinase and glycosidase. On these grounds, we suggest to introduce a final dilution step as indicated above in protocols of sarcoplasmic reticulum membrane preparations.

AMP Deaminase↗
PubMed1982

The effect of trans-stilbene oxide and other structurally related inducers of drug-metabolizing enzymes on glucuronidation.

Administration of trans-stilbene oxide, and new type of inducer of drug-metabolizing enzymes, to rats was found to increase hepatic microsomal UDP-glucuronyl transferase activity with both p-nitrophenol and chloramphenicol as substrate. In Triton X-100 activated microsomes the increase with p-nitrophenol as substrate was to approx. 250% of the control value, while the corresponding value for chloramphenicol was about 600%. These observations indicate that trans-stilbene oxide causes a mixed type 'induction' of UDP-glucuronyl transferase(s), i.e., changes in activity which resemble both those seen after induction with phenobarbital and after treatment with 3-methylcholanthrene. We have also shown that the activity of UDP-glucose dehydrogenase, the enzyme which produces UDP-glucuronic acid, is increased to about 300% of the control after administration of trans-stilbene oxide. The time course of this increase and of the return to control activity after cessation of treatment, the dose-response of this increase and the structural features of the trans-stilbene oxide molecule which are essential for the increase have all been examined. The other two enzymes involved in the conversion of glucose 6-phosphate to UDP-glucuronic acid, namely, phosphoglucomutase and UDP-glucose pyrophosphorylase, were found to be only slightly affected (a 30-60% increase) by treatment with trans-stilbene oxide. After induction with trans-stilbene oxide the hepatic level of UDP-glucuronic acid was unchanged.

Animals↗
PubMed1989

Metabolic regulation during early frog development: glycogenic flux in Xenopus oocytes, eggs, and embryos.

32P-labeled glucose 6-phosphate and phosphoenolpyruvate were injected into oocytes, fertilized eggs, and early embryos of Xenopus laevis, and the 32P label was followed into glycolytic enzymes and acid-soluble metabolites. The kinetics of labeling of phosphoglucomutase and phosphoglyceromutase and the formation of specific metabolites were used to measure carbon flux through glycolytic intermediates in these cells. In full-grown stage VI oocytes, fertilized eggs, and cells of cleaving embryos, carbon metabolism is in the glycogenic direction. Glycolytic intermediates injected into these cells were metabolized into UDP-glucose and then presumably into glycogen. Carbon flow between phosphoenolpyruvate and glucose 6-phosphate does not utilize fructose 1,6-bisphosphatase; rather, it may depend largely on enzymes of the pentose phosphate pathway. Maturation and fertilization of the oocyte did not result in a change in the qualitative pattern of metabolites formed. Pyruvate kinase, although abundant in oocytes and embryos, is essentially inactive in these cells. Pyruvate kinase also appears to be inactive in small previtellogenic stage II oocytes; however, in these cells injected glycolytic intermediates were not metabolized to UDP-glucose.

Animals↗
PubMed1988

Isoenzyme analysis of Echinostoma liei: comparison and hybridization with other African species.

Isoenzyme analysis was carried out on the laboratory strain of Echinostoma liei. The results were compared with those from a preliminary study on Echinostoma caproni, Echinostoma togoensis, and Echinostoma sp. (A. Voltz, J. Richard, B. Pesson, and J. Jourdane, 1986, Annales de Parasitologie Humaine et Comparée, 61, 617-623). Isoelectrofocusing showed characteristic phenotypes for phosphoglucomutase (PGM, EC 5.4.2.2) and glucosephosphate isomerase (GPI, EC 5.3.1.9). The four experimental strains were monomorphic. Their genotypes were defined. Isoenzyme analysis of F1-hybrids and their F2 descendants indicated the subunit structure of both isoenzymes and showed that they were encoded by independent genes. Finally, it also suggested that the four strains corresponded to variants of the same species.

Alleles↗
PubMed1995

Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I.

Carbohydrate-deficient glycoprotein (CDG) syndromes are genetic multisystemic disorders characterized by defective N-glycosylation of serum and cellular proteins. The activity of phosphomannomutase was markedly deficient (< or = 10% of the control activity) in fibroblasts, liver and/or leucocytes of 6 patients with CDG syndrome type I. Other enzymes involved in the conversion of glucose to mannose 1-phosphate, as well as phosphoglucomutase, had normal activities. Phosphomannomutase activity was normal in fibroblasts of 2 patients with CDG syndrome type II. Since this enzyme provides the mannose 1-phosphate required for the initial steps of protein glycosylation, it is concluded that phosphomannomutase deficiency, which is first reported here for higher organisms, is a cause, and most likely the major one, of CDG syndrome type I.

Adult↗
PubMed1993

Species and morphs in the Ostertagiinae: an allozyme study of seven species.

Five enzymes, malate dehydrogenase, lactate dehydrogenase, mannose-phosphate isomerase, glucose-phosphate isomerase and phosphoglucomutase from seven putative species of Ostertagiinae were compared using starch-gel electrophoresis. The Nei distances were not much affected by origin of specimens or host species. Six of the putative species could form polymorphic pairs: Ostertagia ostertagi and Ostertagia lyrata, Ostertagia leptospicularis and Ostertagia kolchida, Teladorsagia circumcincta and Teladorsagia trifurcata. The Nei distance was of the same magnitude (> 0.6) between species pairs, O. ostertagi, O. leptospicularis, T. circumcincta and Spiculopteragia spp.

Animals↗
PubMed1987

Differential loss of enzyme activity by vitC and iron containing proteins.

Our earlier studies showed that rabbit muscle phosphoglucomutase was irreversibly inactivated by exposure to a mixture of vitamin C, FeCl3 and O2. The enzyme lost about 70% of its phosphate (V.V. Desphande and J.G. Joshi, J. Biol. Chem. 260, 754-764, 1985). The present report shows that several other iron proteins can substitute for FeCl3 to a varying degree. The rate of inactivation by FeCl3 greater than ferritin greater than hemoglobin = hemerythrin greater than transferrin = ferridoxin = vitamin C. These iron compounds also produced dephosphoenzyme but did not dephosphorylate ATP, ADP, AMP or phospholipids.

Animals↗