Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Raleigh, North Carolina, population of Drosophila melanogaster was examined for linkage disequilibrium in 1974, several years after previous analyses in 1968, 1969, and 1970. alphaglycerol-3-phosphate dehydrogenase-1 (alphaGpdh-1), malate dehydrogenase-1 (Mdh-1), alcohol dehydrogenase (Adh), and hexokinase-C (Hex-C, tentative name, F. M. Johnson, unpublished; position determined by the present authors to be 2-74.5) were assayed for 617 second chromosomes, and esterase-C (Est-C) and octanol dehydrogenase (Odh) were assayed for 526 third chromosomes. In addition, two polymorphic inversions in the second chromosomes [In(2L)t and In(2R)NS] were examined, and the following findings were obtained: (1) No linkage disequilibrium between isozyme genes was detected. Significant linkage disequilibria were found only between the polymorphic inversions and isozyme genes [In(2L)t vs. Adh, and In(2R)NS vs. Hex-C]. Significant disequilibrium was not detected between In(2L)t and alphaGpdh-1, which is included in the inversion, but a tendency toward disequilibrium was consistently found from 1968 to 1974. The frequency of two-strand double crossovers within inversion In(2L)t involving a single crossover on each side of alphaGpdh-1 was estimated to be 0.00022. Thus, the consistent but not significant linkage disequilibrium between the two factors can be explained by recombination after the inversion occurred. (2) Previously existing linkage disequilibrium between Adh and In(2R)NS (the distance is about 30 cM, but the effective recombination value is about 1.75%) was found to have disappeared. (3) No higher-order linkage disequilibrium was detected. (4) Linkage disequilibrium between Odh and Est-C (the distance of which was estimated to be 0.0058 +/- 0.002) could not be detected (chi(2) (df=1) = 0.9).-From the above results, it was concluded that linkage disequilibria among isozyme genes are very rare in D. melanogaster, so that the Franklin-Lewontin model (Franklin and Lewontin 1970) is not applicable to these genes. The linkage disequilibria between some isozyme genes and polymorphic inversions may be explained by founder effect.
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PMID:The genetic structure of natural populations of Drosophila melanogaster XIII. Further studies on linkage disequilibrium. 40 25

In this communication the results of applying various histochemical semipermeable membrane techniques to the localization of several enzymes in bovine and porcine heart are presented. The Purkinje fibers of the atrioventricular conducting system of the bovine heart differ from the myocardium proper in containing a greater activity of the glycolytic and gluconeogenetic enzymes--lactate dehydrogenase, glyceraldehyde-phosphate dehydrogenase, hexokinase, glucosephosphate isomerase and phosphoglucomutase, and less activity of the aerobic enzymes--NADH: nitroBT oxidoreductase and isocitrate dehydrogenase (NADP+). The metabolic reactions obtained with Purkinje fibers of the porcine heart are less pronounced. These histochemical findings are in accordance with the impression that Purkinje fibers, compared with the common myocardial fibers, have a higher rate of anaerobic metabolism and a lower rate of aerobic metabolism. The activity of the NADPH regenerating enzymes glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating), and the activity of acid hydrolases such as non-specific esterase and acid phosphatase is higher in the Purkinje fibers of both the bovine and porcine heart.
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PMID:Enzyme histochemical studies on the Purkinje fibers of the atrioventricular system of the bovine and porcine hearts. 66 82

Ragweed pollen contains 11 esterase, 5 acid phosphatase, 2 alkaline phosphatose, 2 hexokinase, 2 glucose-6-phosphate dehydrogenase isozymes and one leucine amino peptidase band which can be separated by starch gel electrophoresis. The isozymes were distinguished from one another by their electrophoretic mobility, heat inactivation temperatures and antigenic differences.
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PMID:Characterization of some of the enzymes in ragweed pollen. 127 28

The organ specificity of creatine kinase, esterase, isocitrate dehydrogenase lactate dehydrogenase, nucleoside phosphorylase, adenylate kinase, hexokinase, malate dehydrogenase, malic enzyme, glucose-6-phosphate dehydrogenase of black-white cattle has been studied. Esterases, creatine kinase, adenylate kinase, hexokinase and glucose-6-phosphate dehydrogenase have a very wide spectrum of the organ variabilities. Liver and heart have the largest specificity of enzymes activity. Some peculiarities of isozyme spectrum are found in ovaries and spleen.
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PMID:[Regularities of organ-specific expression of enzyme systems in cattle]. 148 Dec 59

Several enzymes of amino acid and carbohydrate metabolism were studied in primary cultures of fetal rat hepatocytes. One day after plating, activity of both esterase and gamma-glutamyl transpeptidase decreased to half of the freshly isolated hepatocytes, and then remained constant. Acid phosphatase revealed lower activity after plating but recovered to the same levels of isolated cells on day-8. Leucine aminopeptidase and glutathione S-transferase showed a peak of activity respectively on day-6 and day-8. On the other hand, activities of glucose-6-phosphate dehydrogenase, hexokinase and pyruvate kinase increased linearly from Day-1, but only pyruvate kinase reached a plateau on Day-2. These results suggest that different patterns of enzyme activities in the culture might be a reflection, both of a release from homeostatis and adaptation to a new environment.
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PMID:[Enzyme activities in cultured fetal rat hepatocytes]. 286 56

Rats were fed 100 microM AlCl3 for 1 year in their drinking water, then killed and their brains homogenized in 0.1 M Tris (pH 7.4). The 800 g supernatants were assayed for Al3+ and the activities of acetylcholine esterase (ACE), hexokinase and glucose-6-phosphate dehydrogenase (G6PDH). The concentrations of Al in the homogenates, as computed on the original brain for the control and Al fed group were 40 ng and 80 ng/g wet wt, respectively. The activity of ACE was the same in both groups but that of hexokinase and G6PDH in the Al-fed group was about 73% and 80%, respectively, of the control. Dialysis restored the G6PDH but increased the hexokinase of the control group 2-fold and that of Al-fed group 2.7-fold. Thus at this elevated level it was same in both groups. The contribution of Al from the undialysed homogenates during assay was too low to account for the inhibition. It is therefore suggested that a dialyzable inhibitor for hexokinase is normally present in the brain and that Al feeding increases its concentration to further inhibit the utilization of glucose.
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PMID:Effect of long-term feeding of aluminium chloride on hexokinase and glucose-6-phosphate dehydrogenase in the brain. 333 83

A study was made of the enzyme content of the isolated cell walls and of a plasma-membrane preparation obtained by centrifugation after enzymic digestion of the cell walls of baker's yeast. The isolated cell walls showed no hexokinase, alkaline phosphatase, esterase or NADH oxidase activity. It was concluded that these enzymes exist only in the interior of the cell. Further, only a negligible activity of deamidase was detectable in the cell walls. Noticeable amounts of saccharase, phosphatases hydrolysing p-nitrophenyl phosphate, ATP, ADP, thiamin pyrophosphate and PP(i), with optimum activity at pH3-4, and an activity of Mg(2+)-dependent adenosine triphosphatase at neutral pH, were found in the isolated cell walls. During enzymic digestion, the other activities appearing in the cell walls were mostly released into the medium, but the bulk of the Mg(2+)-dependent adenosine triphosphatase remained in the plasma-membrane preparation. Accordingly, it may be assumed that the enzymes released into the medium during digestion are located in the cell wall outside the plasma membrane, whereas the Mg(2+)-dependent adenosine triphosphatase is an enzyme of the plasma membrane. This enzyme differs from the phosphatases with pH optima in the range pH3-4 with regard to location, pH optimum, substrate specificity and different requirement of activators.
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PMID:The enzymic composition of the isolated cell wall and plasma membrane of baker's yeast. 431 24

The technique of isoelectrofocusing has been used to compare culture forms of 12 stocks of T. cruzi isolated in different regions of Venezuela. The following seven enzymes have been used for the characterization: unspecific esterase (E.C.3.1.1), malate dehydrogenase (E.C.1.1.1.37), "malic enzyme" (E.C.1.1.1.40), hexokinase (E.C.2.7.1.1), phosphoglucomutase (E.C.2.7.5.1), glucosephosphate isomerase (E.C.5.3.1.9) and glucose-6-phosphate dehydrogenase (E.C.1.1.1.49). The isoelectrofocusing method allows to determine reproducible enzyme patterns of high selectivity and with a number of bands. This permits to recognize possible differences within the T. cruzi-complex much easier than previous methods. The Venezuelan T. cruzi stocks showed a remarkable homogenous behaviour concerning the enzyme profiles. Most of them were identical. Different types seen for "malic enzyme", phosphoglucomutase, and glucose-6-phosphate dehydrogenase were observed in only three stocks, It was not possible to find a clear relationship between the types and the histories of stocks.
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PMID:The use of isoelectrofocusing in thin layer polyacrylamide and agarose gels as a method for the characterization of Venezuelan Trypanosoma cruzi stocks. 621 77

Aldehyde oxidase (Ao) of Anopheles albimanus Wiedemann was mapped on chromosome 3. The sequence is hexokinase-1--19.2 +/- 1.8--stripe--28.3 +/- 2.2--beta-hydroxy acid dehydrogenase--3.6 +/- 0.3--aldehyde oxidase--2.6 +/- 0.4--esterase-8--6.1 +/- 1.9--esterase-4--?--esterase-6 (phosphoglucomutase). Aldehyde oxidase is 26.1 +/- 2.5 from phosphoglucomutase and 27.2 +/- 1.6 from esterase-6. The one-band electromorph of Ao in homozygotes and the three-band type in heterozygotes suggest that the enzyme is a dimer. The isoelectric points of slow and fast allozymes are 5.5 and 4.8, respectively. A variety of electrophoretic techniques was used to determine if the allozymes of Ao can be differentiated on a basis other than mobility. The slow, fast, and hybrid genotypes were analyzed for differences in thermostability, reactivity to thiol reagent, susceptibility to urea denaturation, substrate specificities, and response to chelating agents. The relative effect of p]H on allozymes was tested by varying the pH of the staining buffer over a range of 4-12. No significant differences were detected among allozymes and no additional allelic variations were observed.
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PMID:Genetic mapping and characterization of aldehyde oxidase of Anopheles albimanus (Diptera: Culicidae). 662 39

beta-Hydroxy acid dehydrogenase (beta-Had-2) of Anopheles albimanus was assigned to chromosome 3. The apparent sequence of loci on chromosome 3 is hexokinase-1--22--stripe--28--beta-hydroxy acid dehydrogenase-2--4--aldehyde oxidase--2--esterase-8--4--esterase-4--?--phosphoglucomutase--?--esterase-6. beta-Hydroxy acid dehydrogenase is 25 and 30 map units from phosphoglucomutase and esterase-6, respectively. The one-band electromorph of beta-Had-2 in homozygotes and the three-band type in heterozygotes suggest that the enzyme is a dimer. A variety of electrophoretic techniques and spectrophotometric analysis were used to determine if the allozymes of beta-Had-2 can be differentiated on a basis other than mobility. No differences were detected among the allozymes on the basis of thermostability, urea denaturation, response to thiol reagents, chelating agents, or changes in coenzyme and substrate concentrations. No heterogeneity within allozymes separated by electrophoresis was detected by using thermostability tests.
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PMID:Genetic and physiochemical studies on beta-hydroxy acid dehydrogenase in Anopheles albimanus. 666 Nov 76


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