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At least 1,243 records · Page 69Linked to original sources
PubMed1980

Leishmania spp. in Iraq. Electrophoretic isoenzyme patterns. I. Visceral leishmaniasis.

Leishmania donovani organisms isolated from 10 children coming from different districts in Iraq, were compared between themselves, with Leishmania donovani isolated in Iran and the Sudan, and with a Leishmania sp. isolated from the viscera of a rat caught in Baghdad. The comparison was made by examination of the electrophoretic mobilities of seven soluble enzymes: malic enzyme E.C.1.1.1.40; glucose phosphate isomerase E.C.5.3.1.9; glucose-6-phosphate dehydrogenase E.C.1.1.1.49; phosphoglucomutase E.C.2.7.5.1.; malate dehydrogenase E.C.1.1.1.37; aspartate aminotransferase E.C.2.6.1.1 and alanine aminotransferase E.C.2.6.1.2 following thin-layer starch-gel electrophoresis. The Iraqi isolations of L. donovani fell clearly into three groups. Group A contained the organisms from seven children, six from the Wasit district and one from the outskirts of Baghdad; Group B, the organism from one child from the Hilla district (100 km south of Baghdad) with severe visceral leishmaniasis which relapsed following chemotherapy; Group C, the organisms from two children from Suaira in the Wasit district. The Iranian and Sudanese isolations gave patterns different from each other and from those from Iran. The Leishmania sp. isolated from the viscera of the rat gave a pattern identical to that of L. tropica.

Animals↗
PubMed1980

Leishmania spp. in Iraq. Electrophoretic isoenzyme patterns. II. Cutaneous leishmaniasis.

Leishmania organisms isolated from the sores of patients in Iraq suffering from cutaneous leishmaniasis were compared between themselves and with Leishmania major, L. tropica and L. donovani, all of which had been identified on clinical and geographical grounds. The comparisons were made by examination of the electrophoretic mobilities of seven soluble enzymes: malic enzyme E.C.1.1.1.40; glucose phosphate isomerase E.C.5.3.1.9; glucose-6-phosphate dehydrogenase E.C.1.1.1.49; phosphoglucomutase E.C.2.7.5.1; malate dehydrogenase E.C.1.1.1.37; aspartate aminotransferase E.C.2.6.1.1 and alanine aminotransferase E.C.2.6.1.2. following thin-layer starch-gel electrophoresis. The Iraqi isolations of Leishmania spp. from cutaneous lesions fell clearly into two groups, one of which gave isoenzyme patterns identical to those of a marker stock of L. major isolated in the USSR, and the other which gave patterns identical to those given by L. tropica also from the USSR. Previously it had been thought that L. tropica alone was responsible for cutaneous leishmaniasis in Iraq. The L. tropica and L. major isoenzyme patterns clearly differentiated these organisms from L. donovani.

Electrophoresis, Starch Gel↗
PubMed1982

A zymodeme study of Entamoeba histolytica in a group of South African schoolchildren.

Using a biphasic culture medium, stocks of intestinal amoebae were isolated from a group of children attending school in Durban, South Africa. These were compared with stocks collected in other areas of the world already characterized using the electrophoretic patterns of four enzymes: glucose phosphate isomerase (GPI), phosphoglucomutase (PGM) L-malate: NADP+ oxido-reductase (oxalacetate-decarboxylating) (ME) and hexokinase (HK). 33% of 94 samples grew Entamoeba histolytica, only one of which gave a pattern indicative of a pathogenic stock. Entamoeba hartmanni, Dientamoeba fragilis and Entamoeba coli were also grown from some samples, increasing the total positive samples for all species isolated to 40%.

Adolescent↗
PubMed1982

The epidemiology of Entamoeba histolytica in a rural and an urban area of Mexico. A pilot survey II.

Stocks of intestinal amoebae grown in monoxenic culture, were compared against each other and against those previously reported from Mexico City. These were isolated from subjects in San Cristobal de las Casas, Chiapas (rural area) and hospital patients in Merida, Yucatan (urban area). Electrophoretic patterns of the four enzymes: glucose phosphate isomerase (GPI), phosphoglucomutase (PGM), L-malate: NADP+ oxido-reductase (oxalacetate-decarboxylating) (ME) and hexokinase (HK) demonstrated the presence of five groups (zymodemes) of Entamoeba histolytica already described from Mexico City, together with two new zymodemes, one of which gave a recognizable pathogenic pattern, whilst the other gave a contradictory pattern. Zymodemes of Entamoeba coli, Entamoeba hartmanni, Iodamoeba buetschlii and Dientamoeba fragilis, previously described were also isolated. One new zymodeme of D. fragilis was demonstrated.

Amebiasis↗
PubMed1983

The presence in Bolivia of two distinct zymodemes of Trypanosoma cruzi, circulating sympatrically in a domestic transmission cycle.

The enzyme profiles of 109 Bolivian stocks of Trypanosoma cruzi were determined by cellulose acetate electrophoresis using the four enzymes: malate dehydrogenase (oxaloacetate decarboxylating) (NADP+) (E.C.1.1.1.40, ME), phosphogluconate dehydrogenase (E.C.1.1.1.44, 6PGDH), phosphoglucomutase (E.C.2.7.5.1, PGM) and glucosephosphate isomerase (E.C.5.3.1.9, GPI). As previously, two principal zymodemes were found sympatrically. Both were isolated from man, one appeared to be more frequent at high altitude, the other appeared to be more frequent at low altitude. These results agree with our previous hypothesis on the genetics of T. cruzi (diploidy, lack of actual sexuality).

Altitude↗
PubMed1987

Further characterization of Leishmania isolates from children with visceral infection in Alexandria area, Egypt.

Two visceral Leishmania isolates from children (aged 1 1/2 and 4 years) living in El Agamy area, Alexandria, Egypt, were compared with 5 marker strains, and 2 other human isolates from Sinai and Sudan, identified on clinical and geographical grounds as cutaneous and visceral leishmaniasis respectively. Isoenzyme variations were assessed on the basis of their electrophoretic profiles on cellulose acetate membranes. The enzymes studied were glucose 6-phosphate dehydrogenase E.C.1.1.1.49, phosphoglucomutase E.C.2.7.5.1, 6-phosphogluconate dehydrogenase E.C.1.1.1.44 (6-PGD), glucose phosphate isomerase E.C.5.3.1.9, malate dehydrogenase E.C.1.1.1.37, mannose phosphate isomerase E.C.5.3.1.8 and nucleoside hydrolase E.C.3.2.2.2. The last 4 enzymes could differentiate between cutaneous and visceral strains. The Alexandria strains proved to belong to the L. donovani complex; however, their 6-PGD pattern was identical to that of L. infantum, which was different from that of the L. donovani marker strain.

Animals↗
PubMedDate not supplied

The substitution of procyclic for bloodstream form Trypanosoma brucei gambiense in isoenzyme studies.

Examination of 10 enzymes from 8 stocks of Trypanosoma brucei showed that procyclic forms could be substituted for bloodstream forms in isoenzyme studies. T. b. gambiense procyclic forms cultured in vitro offer a better source of material for genetic investigations because this species is usually of low infectivity and virulence to laboratory rodents. Using 6 stocks of T. b. gambiense and 2 stocks of T. b. brucei, enzyme patterns of bloodstream and procyclic forms were identical for isocitrate dehydrogenase, malic enzyme, two nucleoside hydrolases (utilizing inosine and deoxyinosine respectively), phosphoglucomutase and superoxide dismutase. Procyclic forms appeared to have greater threonine dehydrogenase activity than bloodstream forms. Consistent differences between bloodstream and culture forms were observed for alanine aminotransferase, aspartate aminotransferase and malate dehydrogenase. These agreed with known differences in the metabolism of procyclic and bloodstream forms.

Animals↗
PubMed1984

Genetic study of high longevity index populations.

Five-year multidisciplinary study of longevity in the Georgian SSR made it possible to select two populations (Abkhazian and Imeretian), in which indices of longevity were much higher, than the average level for the rural population of the whole region. The distribution of polymorphic systems of red cell enzymes (adenilate kinase, esterase D, phosphoglucomutase I, acid phosphatase, 6-phosphogluconate dehydrogenase, glyoxalase I, lactate dehydrogenase, adenosine deaminase, glutamate pyruvate transaminase, phosphoglycolate phosphatase, phosphohexose isomerase) and serum proteins (haptoglobin, Gc-component and transferrin) was studied for genetic analysis of these populations. The results indicate that for all the studied loci the observed genotypic frequencies in both populations are distributed according to Hardy-Weinberg equilibrium. The genetic comparison of the studied populations with some other neighbouring populations did not reveal any genetic peculiarities and the both populations concord with the scheme of anthropological types of Hither Asia. The study of age-related changes of gene frequencies and heterozygosity showed some age-related fluctuations of genetic indices in all age groups, but the heterogeneous nature of these deviations indicate that they may be the result of random genetic processes.

Adolescent↗
PubMed1987

Isolation and partial characterization of the hexokinase isoenzymes from pathogenic and non-pathogenic strains of Entamoeba histolytica.

Isoenzyme electrophoretic patterns (zymodemes) are increasingly used to distinguish between pathogenic and non-pathogenic strains of Entamoeba histolytica. Isolates of E. histolytica from asymptomatic and symptomatic cases have been shown to differ in the electrophoretic mobility of their hexokinase and phosphoglucomutase isoenzymes. The hexokinase isoenzymes from a non-pathogenic strain and from a pathogenic strain of E. histolytica were purified by fast protein liquid chromatography in several steps, which included a separation by size, chromatofocusing, and anion exchange chromatography. The isoenzymes differed in their isoelectric points, which ranged from pH 4.8-5.4, but had very similar kinetic properties and almost identical apparent molecular weights (48,000) in sodium dodecyl sulfate polyacrylamide gels, as well as on gel filtration columns. Comparison of tryptic peptide analysis of each of the isoenzymes indicated considerable homology between the non-pathogenic and pathogenic forms. Antibodies produced against each of the two pathogenic hexokinase isoenzymes inhibited their enzymatic activity. The antibodies also inhibited the activity of the isoenzymes of the non-pathogenic strain. Our findings suggest that the isoenzymes have structural similarities, and that the pathogenic ones differ from the non-pathogenic ones in their electromobility due to post-translational modifications.

Animals↗
PubMed1995

Molecular analysis of two hexokinase isoenzymes from Entamoeba histolytica.

The zymodemes, electrophoretic patterns of hexokinase, phosphoglucomutase and glucose phosphate isomerase isoenzymes, have been widely used to determine the pathogenicity of Entamoeba histolytica isolates. Although pathogenic and nonpathogenic forms of E. histolytica differ clearly in sequences of many homologous genes, a conversion between pathogenic and nonpathogenic zymodemes has been reported by several laboratories. To approach the question what might be the basis for the observed conversion, we examined the molecular biology of the hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) isoenzymes in pathogenic E. histolytica. We isolated two different cDNAs pHXK1 and pHXK2 coding for polypeptides with significant sequence similarity to hexokinases and deduced molecular masses of 49.8 kDa and 49.4 kDa. The two hexokinase sequences differed by 11% on the amino acid and by 8% on the nucleotide level. Expression of the cDNAs in Escherichia coli as nonfusion proteins gave two polypeptides with hexokinase activity. The recombinant Hxk1 and Hxk2 polypeptides comigrated with the more basic and more acidic isoforms of pathogenic amoebae in starch gel electrophoresis, as well as in low and high resolution isoelectric focussing gels. This identified the observed hexokinase isoenzymes of pathogenic E. histolytica as the products of two genes, hxk1 and hxk2.

Amino Acid Sequence↗
PubMed1988

Ferritin: an expanded role in metabolic regulation.

Synthesis of ferritin, a constitutive protein, is increased by iron. This protein is well recognized as a protein which detoxifies, stores and transports iron. The 24 subunits of ferritin assemble to form a protomer of Mr 480,000. This protein shell can sequester up to 4500 g atoms of iron as ferrichydroxyphosphate. Ferritin in vitro and in vivo binds other metal ions such as Cu, Zn, Cd, Pb, Be and Al. Next to Fe it binds large quantities of Be. Therefore, in vitro ferritin protects against and reverses the inhibition by Be of enzymes susceptible to this metal ion. Also, rats pretreated with Fe survive otherwise toxic levels of either pulmonary or intravenous exposure of Be. Liver ferritin from rats injected with Zn contains some of the injected metal ion. Incubation of such ferritin-zinc complex with zinc-requiring apoenzymes restores their activity. Fe(III) of ferritin is released only after its reduction to Fe(II) by a reductant. Incubation of phosphoglucomutase, a phosphoserine containing enzyme with ferritin and a reductant causes irreversible inactivation of the enzyme and removes 70% of its phosphate. Some other phosphoproteins are similarly inactivated but without the loss of the bound phosphate. Thus, uncontrolled release of iron from ferritin, in the presence of a reductant and oxygen can modify several biomolecules and can affect metabolic processes. A subclass of ferritin, acidic isoferritins, have been implicated in leukemia-associated inhibitory activity and has been suggested to inhibit production of Ia+ macrophage progenitors.

Animals↗
PubMed1987

Partial purification and characterization of an aldohexose 1-P phosphatase from pig skeletal muscle.

An enzyme with a molecular weight of 54,000 which possesses phosphatase activity acting on glucose 1-P, galactose 1-P and mannose 1-P has been partially purified and characterized from pig skeletal muscle. The enzyme is free of phosphoglucomutase and galactokinase activities, and it possesses a neutral optimum pH. Pi acts as an inhibitor; glucose, galactose and mannose do not produce any effect. Divalent cations are required for activity, Mg2+ being the most effective activator. Micromolar levels of fluoride and millimolar levels of chloride act as inhibitors; however, vanadate does not produce any effect. The enzyme may have an important role when galactose accumulates in tissues; for example, in galactosemic patients and in young animals ingesting high-galactose diets.

Animals↗
PubMed1985

Enzyme polymorphism in Mansonia uniformis, a mosquito vector of brugian filariasis.

Three temporal samples of a wild population of Mansonia uniformis were analysed for genetic variation at six gene-enzyme systems. Adenylate kinase, hexokinase (3 loci) and cathodal malate dehydrogenase were monomorphic. Phosphoglucomutase, glucose phosphate isomerase, isocitrate dehydrogenase and anodal malate dehydrogenase were polymorphic. Each of the polymorphic loci was represented by three alleles. The average heterozygosity or gene diversity was 0.0437.

Alleles↗
PubMed1988

Metabolism of glucose 1,6-P2--III. Partial purification and characterization of glucose 1,6-P2 synthase from pig skeletal muscle.

1. Glycerate 1,3-P2-dependent glucose, 1,6-P2 synthase has been purified 2000-fold from pig skeletal muscle, with a yield of 75%. 2. The enzyme possesses fructose 1,6-P2-dependent glucose 1,6-P2 synthase and phosphoglucomutase activities, which represent 0.1 and 60% of the main activity, respectively. 3. Both glucose 1-P and glucose 6-P can act as acceptors of the phosphoryl group from glycerate 1,3-P2. 4. The Km values are 19 microM and 67 nM for glucose 1-P and glycerate 1,3-P2, respectively. 5. The enzyme is inhibited by glycerate 2,3-P2, fructose 1,6-P2, glycerate 3-P, phosphoenolpyruvate and lithium, the inhibition pattern varying with the compound.

Animals↗
PubMed1991

Specificity of glucose 1,6-bisphosphate synthesis in rabbit skeletal muscle.

1. To compare glucose 1,6-bisphosphate synthesis in different types of cells, we partially purified (2000-fold) a glycerate 1,3 P2-dependent glucose 1,6-bisphosphate synthase from rabbit skeletal muscle. 2. In agreement with the results reported by others for mouse brain and pig skeletal muscle, the enzyme can be separated from bulk phosphoglucomutase (PGM) activity by DEAE-cellulose chromatography of crude cellular extract. This cannot be achieved on human hemolysates where glycerate 1,3-P2-dependent glucose 1,2-bisphosphate synthesis is displayed only by multifunctional PGM2 isoenzymes. 3. The Km values for glycerate 1,3-P2 (0.50 microM), glucose 1-phosphate (90 microM), Mg2+ (0.22 mM), and also pH optimum (7.8) and mol. wt (70,000) of the rabbit skeletal muscle enzyme are similar to those of the enzymes from mouse brain and human red blood cells, but they differ from those reported for the pig skeletal muscle enzyme.

Animals↗
PubMed1992

Isoenzyme studies in one Brazilian and two Venezuelan strains of Schistosoma mansoni.

1. Enzyme polymorphism, analyzed by starch gel electrophoresis, was found to be zero for acid phosphatase, phosphoglucomutase, phosphoglucose isomerase, glucose 6-phosphate dehydrogenase, lactate dehydrogenase, malate dehydrogenase and malic enzyme, in one Brazilian and two Venezuelan strains of Schistosoma mansoni. 2. All loci studied were monomorphic within strains, but the isoenzymic patterns were, however, different among the strains. 3. Results suggest a drastic loss of the genetic variability usually found in natural populations.

Animals↗
PubMed1991

Isoelectric focusing in immobilized pH gradients: applications in clinical chemistry and forensic analysis.

The applications of isoelectric focusing in immobilized pH gradients in clinical chemistry and forensic analysis are reviewed. Strong emphasis is given to the separation of serum proteins, in particular alpha 1-acidic glycoprotein, acid phosphatase, alkaline phosphatase, alpha 1-antitrypsin, apolipoproteins, complement component, factor B, factor XIIIB, group-specific component, lecithin:cholesterol acyltransferase, phosphoglucomutase, prealbumin, protein C and transferrin. The analysis of human parotid salivary proteins is discussed and an assessment is given of the state of the art in thalassaemia screening.

Blood Proteins↗
PubMed1990

Routine phenotyping of native and desialyzed alpha 2HS-glycoprotein from blood stains.

The application of a polyacrylamide gel isoelectric focusing (PAGIEF) and immunoblotting procedure for the identification of native alpha 2HS-glycoprotein (AHSG) in routine casework blood stains has produced reportable results on 57.2% of samples. This reporting rate is lower than that for group specific component (GC) (83.8%) and phosphoglucomutase (PGM 1) (72.8%) phenotyping of the same samples. Blood stain samples were desialyzed with 1 U/ml neuraminidase, overnight at room temperature prior to PAGIEF in gels containing pharmalyte pH 5-6 and 2.5 M urea. Simple AHSG patterns were developed by immunoblotting. This procedure was five times as sensitive as the native AHSG method and desialyzation was reproducible over a range of incubation times and neuraminidase concentrations. The application of the desialyzed AHSG analysis to routine casework samples has resulted in a significant increase in the number of reportable results (762 reported out of 1027 samples). This reporting rate (74.2%) compares favourably with that for GC (79.1%) and PGH 1 (69.6%) phenotyping of the same samples. The three AHSG alleles (AHSG*1, 2 and 3) are clearly resolved after sample desialyzation and separation in gels containing pharmalyte pH 5-6 and 2.5 M urea. The sensitivity of desialyzed AHSG phenotyping approaches that of GC and this technique is worthy of inclusion in blood stain screening protocols of forensic laboratories in regions where the population has a limited range of rare AHSG alleles.

Blood Proteins↗