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Enzyme
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Query: EC:1.1.1.41 (
isocitrate dehydrogenase
)
3,101
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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.
...
PMID:Enzyme histochemical studies on the Purkinje fibers of the atrioventricular system of the bovine and porcine hearts. 66 82
The dynamics of label distribution was studied in the products of 14CH3OH assimilation by the cells of Pseudomonas gazotropha Z-1156. Substances to be first detected were glycolate, glycine and those of the chromatogram "start" spot. Later, the radioactivity was detected in phosphorylated compounds and glycerate. Cell extracts of Ps. gazotropha Z-1156 contained ribosephosphate isomerase, phosphoribulokinase and glyceraldehyde dehydrogenase but not ribulosediphosphate carboxylase. Distribution of the label in the products of 14CH3OH assimilation and the presence of active hydroxypyruvate reductase in the extract suggest that the serine cycle is involved in methylotrophy of Ps. gazotropha Z-1156. This suggestion is confirmed by the presence of active formate dehydrogenase, phosphoenolpyruvate carboxylase, (
NADP+
, Mn2+)-specific
isocitrate dehydrogenase
, (NAD, Mg2+)-specific malate dehydrogenase, malate lyase, and isocitrate lyase. The citric acid cycle is open at the alpha-ketoglutarate dehydrogenase system. The dry biomass of Ps. gazotropha Z-1156 contains over 70% of protein.
...
PMID:[Carbon assimilation pathways in the methylotrophy of Pseudomonas gazotropha]. 70 43
Streptozotocin-induced diabetes suppressed the normal development of the nine glycolytic and lipogenic enzyme activities measured. With the exception of
NADP
-
isocitrate dehydrogenase
, insulin replacement therapy induced increased activities of the enzymes in streptozotocin-treated rats. Insulin appeared to have a specific effect on the activities of glucokinase, ATP-citrate lyase, malic enzyme, and glucose-6-P-dehydrogenase.
...
PMID:Effect of streptozotocin diabetes and insulin administration on some liver enzyme activities in the post-weaning rat. 72 37
The specific activity of human platelet monoamine oxidase from control subjects undergoing glucose tolerance tests is reduced drastically. Three hours after intake of 100 g of glucose only 25%-30% of the MAO-baseline activity was measured with tryptamine. beta-phenylethylamine and p-tyramine as substrates. At about 5 hr, platelet MAO activity has increased again. Inhibition was not due to small molecular weight inhibitors or other diffusible factors. Studies of other platelet enzymes, including succinate dehydrogenase and
isocitrate dehydrogenase
(
NADP+
dependent) showed no parallel reductions; hGH, insulin, blood glucose and platelet glycogen concentrations did not correlate with platelet MAO activity. The changes of MAO activity in respect with p-tyramine and tryptamine as substrates 24 hr after glucose ingestion suggest changes of the lipid microenvironment of this enzyme of the outer mitochondrial membrane.
...
PMID:Factors altering platelet monoamine oxidase. The influence of oral glucose intake. 76 48
The specific activity of a peroxisomal enzyme, lactate oxidase, and of pyruvate kinase and lactate dehydrogenase, which are not peroxisomal, increased rapidly when shaken cultures of Tetrahymena were transferred to conditions of oxygen restriction and supplemented with glucose. Two other peroxisomal enzymes, catalase and
TPN
-linked
isocitrate dehydrogenase
, did not increase substantially, nor did succinate dehydrogenase. The increases were reduced if glucose was not added at the time of transfer, and were prevented by actinomycin D or cycloheximide, but not by chloramphenicol. The results suggest an involvement of peroxisomes in the metabolism of glycolytic endproducts when the availability of oxygen to the cell is limiting.
...
PMID:Synthesis of glycolytic and peroxisomal enzymes in Tetrahymena following a change in culture conditions. 80 70
This paper presents preliminary data concerning the relationship of various components of glandular epithelium and effect of enzymes on metabolism, storage, and release of certain substances in normal and abnormal endometria. Activity of these endometrial enzymes has been compared between two groups: 252 patients with normal menstrual histories and 156 patients, all over the age of 40, with abnormal uterine bleeding. Material was obtained by endometrial biopsy or curettage. In the pathologic classification of the group of 156, 30 patients had secretory endometria, 88 patients had endometria classified as proliferative, 24 were classified as endometrial hyperplasia, and 14 were classified as adenocarcinoma. All tissue was studied by histologic, histochemical, and biochemical methods. Glycogen synthetase activity caused synthesis of glucose to glycogen, increasing in amount until midcycle, when glycogen phosphorylase activity caused the breakdown to glucose during the regressive stage of endometrial activity. This normal cyclic activity did not occur in the abnormal endometria, where activity of both enzymes continued at low constant tempo. Only the I form of glycogen synthetase increased as the tissue became more hyperplastic. With the constant glycogen content and the increased activity of both the
TPN
isocitric dehydrogenase
and glucose-6-phosphate dehydrogenase in the hyperplastic and cancerous endometria, tissue energy was created, resulting in abnormal cell proliferation. These altered biochemical and cellular activities may be the basis for malignant cell growth.
...
PMID:The effect of enzymes upon metabolism, storage, and release of carbohydrates in normal and abnormal endometria. 81 24
In order to assess the extent to which metabolism within the sheep placenta may influence the transfer of metabolites between mother and foetus at different stages of gestation the activities of enzymes concerned with some aspects of carbohydrate, amino acid and keton body metabolism were determined in placental cotyledons resected from ewes during the last three months of pregnancy. The activities of pyruvate kinase (EC 2.7.1.40), lactate dehydrogenase (EC 1.1.1.27), malate dehydrogenase (EC 1.1.1.37), ATP citrate (pro-3S)-lyase (EC 4.1.3.8), citrate (si)-synthase (EC 4.1.3.7), acetyl-CoA synthetase (EC 6.2.1.1), acetyl-CoA acetyltransferase (EC 2.3.1.9) and 3-keto acid CoA-transferase (EC 2.8.3.5) per gram wet weight cotyledon do not change during the period studied. The activities of alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1),
isocitrate dehydrogenase
(
NADP+
) (EC 1.1.1.42), ornithine-oxoacid aminotransferase (EC 2.6.1.13) and 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) show an increase in activity between the third and fourth months of pregnancy whilst the activities of arginase (EC 3.5.3.1) and possibly pyruvate carboxylase (EC 6.4.1.1) show an increase in activity between the fourth and final months of pregnancy. Ornithine decarboxylase (EC 4.1.1.17) activity declines to one tenth of its activity during this later period. The absence of detectable activities of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) and ornithine carbamoyltransferase (EC 2.1.3.3) indicate that gluconeogenesis and urea synthesis from ammonia do not occur in the sheep placenta. It appears that the ability of the placenta to metabolise several substrates is achieved by the time the placenta reaches its maximum size at approximately 90 days.
...
PMID:Enzyme activities in the sheep placenta during the last three months of pregnancy. 84 73
DL-threo-alpha-Methylisocitrate (3-hydroxy-1,2,3-butanetricarboxylate) is a substrate for bovine heart aconitase and an inhibitor of
TPN
-linked
isocitrate dehydrogenase
from liver and heart. The isomer of alpha-methylisocitrate formed from alpha-methyl-cis-aconitate (cis-2-butane-1,2,3-tricarboxylate) by aconitase inhibits
TPN
-linked
isocitrate dehydrogenase
and has been identified as D-threo-alpha-methylisocitrate (2S,3R)-3-hydroxy-1,2,3-butanetricarboxylate) by optical rotation and circular dichroism studies. Mitochondrial bovine heart aconitase catalyzes a reversible reaction between D-threo-alpha-methylisocitrate (Km, 0.2 mM) and alpha-methyl-cis-aconitate (Km, 0.05 mM) at pH 7.4. However, formation of methylcitrate (2-hydroxy-1,2,3-butanetricarboxylate) from these substrates or utilization of synthetic methylcitrate for formation of these products could not be demonstrated with bovine heart aconitase. DL-threo-alpha-Methylisocitrate is also a substrate for aconitase from rat liver cytosol (Km, 0.1 mM); Vmax with citrate is approximately 1.4 times that with DL-threo-alpha-methylisocitrate. The ratio of activities for these substrates observed with the bovine heart enzyme is about 5. Formation of alpha-methyl-cis-aconitate from synthetic methylcitrate could not be detected spectrophotometrically with the liver aconitase; if it occurs with either the liver or the heart enzyme, the rate would be less than 0.1% that obtained with DL-threo-alpha-methylisocitrate. A new synthesis of methylcitric acid in good yields from diethyl alpha-methyl-beta-ketoglutarate (diethyl 2-methyl-3-oxoglutarate) and cyanide has been described. NMR spectroscopy indicates that this synthetic methylcitric acid contains the two racemic pairs of diastereoisomers.
...
PMID:Identification of D-threo-alpha-methylisocitrate as stereochemically specific substrate for bovine heart aconitase and inhibitor of TPN-linked isocitrate dehydrogenase. 85 1
In the presented study the influence of freezing and freeze-drying on enzyme activity is described. Attention is paid to 16 enzymes which can be used for quantitative enzyme histochemical techniques. With the exception of succinate dehydrogenase only, no significant inactivation during freezing and freeze-drying procedures could be demonstrated with lactate dehydrogenase, malate dehydrogenase (NAD+), malate dehydrogenase (decarboxylating) (
NADP+
),
isocitrate dehydrogenase
(
NADP+
), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADH-oxydoreductase, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome c oxidase, phosphoglucomutase, glucosephosphate isomerase, glucose-6-phosphatase, acid phosphatase, beta-glucuronidase and non specific aryl esterase. Therefore, the results supply a sound foundation for those quantitative enzyme histochemical techniques in which tissue specimens are frozen or frozen-dried before enzyme estimations are performed.
...
PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61
Specific activities of
NADP
isocitrate dehydrogenase
and acetylcholinesterase were significantly higher in muscle fibres differentiated, in vitro, from myoblasts of adductor magnus (red) than pectoralis major (white) muscles 10-day-old chick embryos. This is evidence, as far as enzyme activities are concerned, that myoblasts from different types of skeletal muscles are able to give, in tissue culture, muscle fibres of different properties, even in the absence of nerve supply.
...
PMID:Enzymatic activities of muscle fibres differentiated, in vitro, from pectoralis major (white) and adductor magnus (red) muscles of chick embryos. 89 21
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