Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of glycolysis and glyconeogenesis enzymes, content of carbohydrate and nitrogen compounds were studied in muscles of 15-month cattle of different sex of the black-piebald breed and its crosses with bulls of two meat breeds Hereford and Limousine. In the muscles of bulls the activity of phosphoglucomutase, phosphohexoisomerase, aldolase and fructose-1,6-diphosphatase is considerably higher (except of the activity of phosphoglucomutase and phosphohexoisomerase in the muscles of pure-bred black-piebald animals for which difference is not statistically reliable) and the content of glycogen, glucose, fructose, lactic acid, free and phosphorylated pentoses of nonadenylic compounds is essentially lower than in the muscle tissue of heifers of analogous breed groups. A higher activity of carbohydrate metabolism enzymes (especially aldolase and fructose-1,6-diphosphate) and a higher content of total pentoses, the adenylic system pentoses, ATP phosphorus in the muscles of the cross Limousine and Hereford bulls and Limousine heifers as compared to the pure-bred black-piebald animals of the corresponding sex coincide with a greater increase in the muscular tissue and more intensive synthesis of proteins in it. A considerably lower level of glycogen, glucose, fructose and a relatively high activity of carbohydrate metabolism enzymes in the muscles of cross young cattle show that disintegration of these carbohydrates is in excess of their synthesis, that is due to an increase in the energy demand connected with a more intensive synthesis of proteins in the muscular tissue. Therefore, in the authors opinion the performed kill of the cross Limousine and Hereford bulls as well as Limousine heifers, is somewhat untimely and unreasonable. At the same time the activity of all the studied enzymes in the muscles of the cross Hereford heifers, vice versa, is considerably lower as compared to the black-piebald heifers and coincides with a low gain in live weight and muscular tissue, a more rapid accumulation of glycogen and lipids and a more delayed--of proteins in the muscular tissue, that evidences for their early maturity. Therefore the further raising of the cross Hereford heifers in the farm for obtaining meat is economically less profitable. The data obtained give grounds to recommend determination of the activity of carbohydrate metabolism enzymes, especially of aldolase and fructose-1,6-diphosphate, as a test for checking the muscular tissue growth and for prognosing the meat productivity in the growing pure-bred and cross young cattle of different sex.
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PMID:[Activity of carbohydrate-metabolizing enzymes and content of carbohydrate and nitrogen compounds in muscles of young cattle depending on breed and sex]. 17 55

Studied were the changes in the values of some hematologic indices (hemoglobin, erythrocytes, leukocites) as well as the values of some biochemical (total protein and protein fractions, urea, total lipids, bilirubin, inorganic, phosphorus calcium) and enzyme factors (lactatedehydrogenase, alkaline and acid phosphatase, aldolase, amino transferrases, creatinephosphokinase) in geese prior to and after experimental infection of Borrelia anserina. It was found that in the peak stage of spirochetemia the content of hemoglobin, total lipids, and calcium, the percent of albumins and alfa-globulins, and the activity of the alkaline phosphatase in the blood decreased. The prealbumin fraction of the serum protein was completely reduced. The activity of the lactatedehydrogenase, acid phosphatase, amino transferrases, and aldolase showed higher values that were statistically significant, while the activity of the creatinephosphokinase rose to a slighter extent. The urea, bilirubin, inorganic phosphorus, and the alfa-, beta-, and gamma-globulins correlated positively with the course of the infection.
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PMID:[Biochemical changes in the blood of geese infected with Borrelia anserina]. 117 37

N-(omega-Hydroxyalkyl)glycolamidobisphosphoric esters (P-O-CH2-CO-NH-(CH2)n -O-P), which are analogues of the aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) substrate fructose 1,6-bisphosphate, were synthesized and used for probing its active site. These phosphate compounds competitively inhibited aldolase activity. The Ki value was lowest when the maximum distance between the phosphorus atoms of the bisphosphate was brought close to that of fructose 1,6-bisphosphate. The inhibitor constants, Ki, were compared to those of alkanediol monoglycolate bisphosphoric esters and alkanediol bisphosphate compounds, which were reported previously by Ogata et al. The values of Ki for the bisphosphate compounds containing an amide group, the amide bisphosphate compounds, were smaller than those for the bisphosphate compounds containing an ester group, the ester bisphosphate compounds, and those for alkanediol bisphosphates were the largest for the same distance between phosphorus atoms in these bisphosphates. The difference spectra of aldolase caused by binding of a saturating concentration of N-(omega-hydroxypropyl)glycolamidobisphosphoric ester resembled that of butanediol monoglycolate bisphosphoric ester. However, the effects of the amide bisphosphate compounds on the absorption spectrum of aldolase were smaller than those of the ester bisphosphate compounds for the same distance between phosphorus atoms in these bisphosphate compounds. These results suggest that the synthesized phosphate compounds bind to aldolase at the active site and the -CO-NH- group of the compounds might be held more tightly than the -CO-O- group by hydrogen bonds, presumably with the amino acid residues in the active site, such as Lys-146 or -229 and Asp-33 or Glu-187. On the other hand, the -CO-O- group might be more effective in changing the environment of the Trp-147 residue in the active site of this enzyme.
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PMID:An exploration of the binding site of aldolase using N-(omega-hydroxyalkyl) glycolamidobisphosphoric esters. 226 71

The reproducibility of the studied biochemical methods was determined by means of the criterion of dispersion of the results approaching the average arithmetic value--the coefficient of variance 'V'. A total of thirty analyses per series were made of one and the same sample, under one and the same conditions, by one and the same laboratory assistant. The blood plasma of cows was studied spectro-photometrically with regard to the levels of urea, total protein, sialic acids inorganic phosphorus, carotene, cholesterin, alkaline phosphatase, aldolase, GOT, GPT, and whole blood (for blood sugar). Complexonometrically, blood plasma was studied for total calcium and magnesium. Flame-photometrically, blood plasma was studied for the content of potassium and sodium; these elements were also followed up in erythrocytes and urine of cows as well as in semen of boars. Employed were methods that were routinely used within the system of the Research and Productional Veterinary Union as suggested by Tsvetkov et al. in their Manual of Methodical Guidance. The values of the coefficient of variance for the variance series of each index were compared to the admissible boundary of V (AB-V) as calculated by Tonks' method. Stated are the sources of mistakes for each of the methods tested, and possibilities are sought to optimize the values of V through eliminating accidental errors.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Reproducibility of spectrophotometric and flame photometric methods]. 409 Feb 65

Hereditary fructose intolerance (HFI) is a potentially life-threatening disorder and can be suspected from a detailed nutritional history. The usefulness of 2 diagnostic procedures, fructose tolerance test (FTT) and aldolase assay on biopsied liver, was studied. A standardized intravenous FTT with 200 mg/kg b.w. was done on 11 children with HFI, 17 age-matched contrast children, 6 adults with HFI and 6 adult controls. Blood glucose, phosphorus, urate, magnesium and fructose were followed for 2 hours. By the FTT, each HFI individual was reliably distinguished from controls and contrasts and even from those with acute liver disease other than HFI. Both children with non-HFI hepatopathy examined by both procedures had a normal FTT in spite of reduced liver fructaldolase activity. HFI children responded to the FTT by earlier and more pronounced hypoglycemia than adults, and one girl converted to an adult type response between the ages 12 and 181/2 years. Responses of two HFI sibling pairs and of one set of monozygotic twins were typical for age, but resemblance was no greater than within the unrelated HFI probands. The intravenous FTT is judged a reliable diagnostic tool, simple and harmless if done in hospital. Essential fructosuria is readily diagnosed by the FTT, but fructose-1,6-diphosphatase deficiency and HFI are not differentiated with certainty. Liver biopsies were obtained from 35 children with HFI, 14 contrast persons and 10 controls (of which 9 organ donors) and examined enzymatically. Deficiency of fructaldolase was observed in all HFI children but also in some contrast children suffering from acute liver disease other than HFI. In these, HFI could only be excluded when the reduced activity of reference enzymes such as fructose-1,6-diphosphatase and glucose-6-phosphatase and liver histology were included in the evaluation. In one deceased HFI infant, fructaldolase was deficient in both, liver and kidney cortex. Extent of antibody activation and of heat inactivation of residual fructaldolase varied between unrelated HFI patients but not within families. These results did not contribute to diagnosis but further documented genetic heterogeneity of HFI. For diagnosis of HFI we recommend 1. immediate elimination of fructose from the diet, 2. the intravenous FTT after several weeks of fructose withdrawal, and 3., should diagnosis still be uncertain, laparoscopic liver biopsy for assay of fructaldose and of reference enzymes and for histology.
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PMID:The diagnosis of hereditary fructose intolerance. 626 73

Investigations were carried out with a total of 276 high-producing and clinically healthy cows that had freshly calved on 11 farms, being divided into groups according to the extent to which ketonuria was present if al all. Whole blood and blood serum were sampled to determine the ketone bodies, blood sugar, erythrocyte and leukocyte counts, hemoglobin, inorganic phosphorus, Ca, Mg, total protein, carotene, and activity of the GOT and GPT enzymes as well as the activity of lactic acid dehydrogenase, alkaline phosphatase, aldolase, and leucine aminopeptidase. Studied were the body temperature, the pulse rate, and the respiration rate. It was found that on farms with ketosis in cows ketonuria was manifested most often after the ketone bodies in the blood rose to 10-12 mg%. At the same time the blood sugar level was lowered and as a rule it showed reverse correlation with the levels of ketonemia and ketonuria. In such cows there was a lowering trend with the Ca and carotene contents and the erythrocyte count, and the respiration rate was higher. There were no changes in the body temperature, pulse rate, leukocyte count, Ca, Mg, hemoglobin, protein, and the activity of aldolase. The activity of the other enzymes mentioned was higher, and it correlated positively with the rise of ketonemia and ketonuria. With diseased cows the activity of alkaline phosphatase only was shown to be lower, negatively correlating with ketonuria.
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PMID:[Changes in the serum enzymes and clinical and clinico-biochemical indices of cows with subclinical ketosis]. 653 57

Alkanediol monoglycolate bisphosphoric esters (P-O-CH2-CO-O-(CH2)n-O-P), which are analogues of the aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) substrate fructose 1,6-bisphosphate, were synthesized and used for probing its active site. The Ki value was lowest when the maximum distance between the phosphorus atoms of the bisphosphate was brought close to that of fructose 1,6-bisphosphate. The binding constants estimated from difference spectra correlate well with Ki values for the substrate analogues. Propanediol monoglycolate bisphosphoric ester protected aldolase from inactivation by 1,2-cyclohexanedione, which preferentially attacks arginine-55. However, propanol phosphate had little protective effect. The synthesized phosphate compounds protected the enzyme against inactivation by trypsin, and also against spontaneous denaturation. These results suggest that the synthesized phosphate compounds bind to aldolase at the active site, which tends to keep the distance constant between the two phosphate-binding sites for the open-chain form of fructose 1,6-bisphosphate, and stabilize the natural conformation of the enzyme. Both arginine-55 and lysine-146 are shown to participate in the phosphate-binding site for the C-1-phosphate of fructose 1,6-bisphosphate.
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PMID:An exploration of the binding site of aldolase using alkanediol monoglycolate bisphosphoric esters. 682 94

We examined the kinetics study of serum enzyme after the administration of beta-blocking agents or alpha-stimulator in the experimental rats. Following the administration of beta-blocking agents, propranolol and pindolol, the serum levels of adenylate kinase, aldolase, lactate dehydrogenase and aspartate aminotransferase as well as that of creatine kinase increased in rats. The same was observed following the administration of noradrenaline (an alpha-stimulator). Isoenzyme pattern indicated that most of these enzymes were considered to be released from muscular tissues. There were also changes in serum calcium, inorganic phosphorus and magnesium, concurrently with the release of the enzymes into the serum.
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PMID:Effects of beta-blocking agents on the release of various enzymes in muscular tissues. 796 81

Glucose and phosphorus metabolism in mature (8-month-old) rat lenses were examined with NMR spectroscopy. Nondiabetic mature lenses contained sorbitol-3-phosphate (S3P) and fructose-3-phosphate (F3P) which were absent from young (1- to 2-month-old) normal rat lenses. The concentrations of these two phosphates can be changed through (1) diabetes induction with streptozotocin - this results in a dramatic increase in both compounds; and (2) oral dosing with a drug known to prevent sorbitol production - both metabolites disappeared. When normal mature lenses were incubated in 35.5 mM 13C1-glucose, both 13C1-lactate and 13C3-lactate were produced. Preservation of the 13C label at C1 is likely through the formation of 13C1-S3P and -F3P, which were then split through an aldolase-like mechanism into two 3-carbon compounds, one an unlabeled glycerol and the other 13C1-alpha-glycerophosphate (from S3P) and 13C1-dihydroxyacetone phosphate (from F3P). These reactions can contribute to the increase in alpha-glycerophosphate observed in both the streptozotocin-induced diabetic lenses and lenses incubated in high glucose.
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PMID:The further metabolism of sorbitol-3-phosphate and fructose-3-phosphate in the mature rat lens. 872 78

In vivo 31Phosphorus magnetic resonance spectroscopy (31P-MRS) permits evaluation of dynamic changes of individual phosphorus-containing metabolites in the liver parenchyma, such as phosphomonoester (PME), adenosine triphosphate, and inorganic phosphate (Pi). Intravenous fructose load alters phosphorus metabolites and allows assessment of liver function by 31P-MRS. 31P-MRS data obtained in alcoholic liver disease are however inconclusive. To study the hypothesis that fructose load can be used to investigate metabolic effects of ethanol ingestion, the interaction of different metabolites--i.e., fructose and ethanol--were followed in vivo. Using a 1.5 Tesla magnetic resonance system, six healthy volunteers were examined in three sessions each: a session after administration of (a) fructose only (250 mg/kg) was compared with (b) fructose load after ethanol ingestion (0.8 g/kg). A control experiment (c) was done after ethanol only. Spectra were acquired using one-dimensional chemical shift imaging with a temporal resolution of 5 min. Following a fructose load, the concomitant uptake of ethanol showed drastic changes of individual metabolic steps of the hepatic metabolism (averages +/- standard deviation). While the velocity of the net formation of PME (relative increase 0.46 +/- 0.11 without ethanol vs. 0.61 +/- 0.25 with ethanol) and the use of adenosine triphosphate (-0.13 +/- 0.03 vs. -0.16 +/- 0.03) and Pi (-0.022 +/- 0.009 vs. -0.021 +/- 0.004) were not significantly affected by ethanol uptake, a significant (p < 0.01) reduction of PME degradation (31.3 +/- 9.4 vs. 61.9 +/- 16.9 relative total area) and absence of an overshoot for Pi (10.5 +/- 4.9 vs. -7.1 +/- 5.3 relative area 13 min to 43 min) was observed after ethanol administration. Dynamic 31P-MRS allows the observation of individual steps of hepatic metabolism in situ; fructose metabolism in the human liver is slowed down by concomitant ethanol ingestion after the phosphorylation step of fructose. This could be explained by inhibition of aldolase rather than ethanol-induced changes of the hepatic redox state. Fructose load can be used to study effects of alcohol ingestion and might therefore be useful in patients with alcoholic liver disease.
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PMID:Effect of ethanol and fructose on liver metabolism: a dynamic 31Phosphorus magnetic resonance spectroscopy study in normal volunteers. 936 53


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