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

---

Query: EC:1.1.1.41 (isocitrate dehydrogenase)
3,101 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzyme electrophoretic variants were studied in 49 strains of Vibrio cholerae using zymovar analysis. The following seven enzymes were selected for use: alanine dehydrogenase (ADH), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH), phosphoglucomutase (PGM), glucosephosphate isomerase (GPI), 6-phosphogluconate dehydrogenase (6PGDH) and glucose-6-phosphate dehydrogenase (G6PDH). The results indicated the presence of three main groups defined chiefly by their GPI and 6PGDH variants. The first group, defined by possessing the variants GPI-2 and 6PGDH-3, contained all the 01 serovar and E1T or biovar isolates from cholera cases. The second group, defined by possessing the variants GPI-3 and 6PGDH-2, contained all the 01 serovar and classical biovar isolates; the third group was heterogeneous and included the 01 serovar isolates from environmental sources as well as isolates of other serovars (the so called NAGs, non-agglutinable with 01 antisera or NCVs). It is thus now possible to separate the epidemic strains of 01 serovar from other members of this serovar isolated from the environment. Zymovar analysis deals with differences which are a direct expression of the genome and seems to be unaffected by gross phenotypic changes such as smooth-rough variation and phage resistance. It is a promising tool for investigating bacteriological and epidemiological questions, in particular the significance of an environmental reservoir of cholera.
...
PMID:Enzyme markers for Vibrio cholerae: identification of classical, El Tor and environmental strains. 293 9

The aim of the present study was to evaluate the effects of medroxyprogesterone acetate (MPA), an inducer of liver drug metabolism, on the ability of liver to generate NADPH, a reducing cofactor for drug oxidation reactions in normal rats and to compare these results with those obtained in rats receiving phenobarbital (PB), a well known inducer of liver drug metabolism. The results showed that: 1. Administration of MPA (100 mg/kg body wt) for a week increased liver wt and NADPH cytochrome P-450 reductase activity, suggesting that the compound induced liver drug metabolism. 2. The regimen also increased the activities of two NADPH generating enzymes, isocitrate dehydrogenase and malic enzyme, suggesting that MPA enhanced the capacity of normal liver tissue to produce NADPH. 3. Phenobarbital treatment increased the activities of three NADPH generating enzymes, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and malic enzyme, suggesting that MPA and PB differ in their effects on the liver NADPH-producing system.
...
PMID:Medroxyprogesterone acetate (MPA) enhances liver NADPH-generating enzyme activities in normal rats. 297 Sep 86

The administration of medroxyprogesterone acetate (MPA) and phenobarbital (PB) improves liver function in rats with liver damage. This was seen here as increased aryl hydrocarbon hydroxylase (AHH) activity after therapy with MPA or PB in rats with a chemical liver injury, produced by dimethylnitrosamine (DMN). Hepatic glucose-6-phosphatase (G6Pase) activity, an index of glucose metabolism was also normalized in the MPA treated rats. The present study further shows that MPA induced hepatic malic enzyme (ME) and isocitrate dehydrogenase (ICDH) activities and PB enhanced glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and ME activities in the DMN pretreated rats. This suggests that MPA and PB enhanced the capacity of altered liver tissue to generate NADPH, a cofactor in the monooxygenase system, which may, in part, enhance the restoration of drug hydroxylation in the rats. Since G6PDH, 6PGDH and ME participate in glucose metabolism, the finding that the compounds influenced these enzymes in distinct ways, may explain the different effects of MPA and PB on the restoration of glucose metabolism.
...
PMID:Medroxyprogesterone acetate and phenobarbital induce NADPH producing enzyme activities in rats with a chemical liver injury. 300 83

Equilibrium constants for reactions catalyzed by ribulose-5-phosphate 3-epimerase, [sigma xylulose-5-P]/[sigma ribulose-5-P] = 1.82, ribose-5-phosphate isomerase, [sigma Rib-5-P]/[sigma ribulose-5-P] = 1.20, transaldolase, [sigma erythrose-4-P] [sigma Fru-6-P]/[sigma sedoheptulose-7-P] [sigma glyceraldehyde 3-P] = 0.37, and transketolase, [sigma Fru-6-P] [sigma glyceraldehyde 3-P]/[sigma erythrose-4-P] [sigma xylulose-5-P] = 29.7 and [sigma Rib-5-P] [sigma xylulose-5-P]/[sigma sedoheptulose-7-P] [sigma glyceraldehyde 3-P] = 0.48, were redetermined under physiological conditions. The equilibrium constant for the combined glucose-6-P dehydrogenase and 6-phosphoglucono-gamma-lactonase reaction, [6-phosphogluconate3-] [NADPH] [H+]2/[Glc-6-P2-] [NADP+], was found to be at least 1 X 10(-9). Using these redetermined equilibrium constants, calculated values of pentose cycle intermediates, based on near equilibrium assumptions and the tissue content of Fru-6-P and glyceraldehyde 3-P, were found to be in good agreement with measured values for male Wistar rats injected with saline, 20 mumol/g pyruvate, 20 mumol/g gluconate, and 20 mumol/g ribose. Measured and calculated values for pentose cycle intermediates in saline injected animals were ribulose-5-P; 3.8 +/- 0.4 and 2.4 +/- 0.1 nmol/g; xylulose-5-P, 5.9 +/- 0.6 nmol/g and 4.3 +/- 0.2 nmol/g; sedoheptulose-7-P, 41.5 +/- 2.4 and 37.6 +/- 2.9 nmol/g; and combined sedopheptulose-7-P and Rib-5-P, 43.0 +/- 2.8 nmol/g and 40.5 +/- 3.0 nmol/g; liver content of erythrose-4-P was less than the detection limits of the assay, 2 nmol/g. Calculated erythrose-4-P was 0.23 +/- 0.01 nmol/g. Liver content of 6-phosphogluconate was 8.5 +/- 0.7 nmol/g. The free cytosolic [NADP+]/[NADPH] ratio calculated from the 6-phosphogluconate dehydrogenase redox couple, 0.0030 +/- 0.0002, was also in good agreement with that calculated from the malic enzyme redox couple, 0.0051 +/- 0.0007, and the isocitrate dehydrogenase redox couple, 0.0066 +/- 0.0008. These data indicate the interdependence of the liver content of glycolytic intermediates and pentose cycle intermediates in ad libitum fed rats.
...
PMID:The interdependence of glycolytic and pentose cycle intermediates in ad libitum fed rats. 307 59

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
...
PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

Alkaline phosphatase (Alp), esterase-I (Es-I), esterase-II (Es-II), carbonic anhydrase (CA), cell esterase (cEs), esterase-D (Es-D), isocitrate dehydrogenase (ICD), malate dehydrogenase (MDH), 6-phosphogluconate dehydrogenase (PGD), tetrazolium oxidase (To), ceruloplasmin (Cp), Haptoglobin (Hp) and hemoglobin (Hb) in 58-75 samples of three species of tamarins (Saguinus mystax, S. labiatus and S. oedipus) were detected by means of horizontal starch gel electrophoresis. Two types (Es-I 1 and Es-I 2) for Es-I, four types (Es-II 1, Es-II 2, Es-II 3 and Es-II 2-3) for Es-II, three types (cEs 1, cEs 2 and cEs 1-2) for cEs, three types (PGD 1, PGD 2 and PGD 1-2) for PGD, two types (To 1 and To 2) for To, and three types (Hp 3, Hp 1-3 and Hp 2-3) for Hp were observed. However, Alp, CA, Es-D, ICD, MDH, Cp and Hb were monomorphic. In the S. mystax, no Es-II or PGD variants were observed. No Es-II variant was seen in the S. oedipus. Gene frequencies of cEs, PGD and Hb were biased in the three species. It is concluded that six polymorphic loci are useful as genetic markers for a species or individual.
...
PMID:Genetic markers in the blood of three species of tamarins (Saguinus mystax, S. labiatus and S. oedipus). 310 Mar 16

Acclimation of carp both to the temperature fall (from 20 to 5 degrees C) and rise (from 20 to 30 degrees C) induces an increase in activity of cytoplasmic liver NADPH-generating enzymes--glucose-6-phosphate dehydrogenase (G6PDG) and malic-enzyme (ME) 6-phosphogluconate dehydrogenase (6PGDG) and NADP-isocitrate dehydrogenase (NADP-IDG) activities are unchanged. Actinomycin D does not prevent cold activation of G6PDG but blocks activation of ME. "Warm" G6PDG has minimal Km value for glucose-6-phosphate and "warm" ME has minimal Km value for glucose-6-phosphate and "warm" ME has minimal Km value for malate at 25 degrees C "Cold" G6PDG and ME have the warmest Km values at 5 degrees C. Isozyme composition of cytoplasmic G6PDG (2 bands with Rf 0.16 and 0.20) does not change within the limits of 5-30 degrees C. The prolactin action on G6PDG and ME is similar to the effect of cold acclimation (activity increases Km value decreases, isozyme pattern (for G6PDG) remains unchanged). It is supposed that activation of G6PDG and ME during cold adaptation may be a result of the prolactin action on substrate-binding ability without changes in the enzyme biosynthesis and isozyme pattern.
...
PMID:[The effect of temperature acclimation on NADP-dependent dehydrogenase activity in the carp liver and various mechanisms of its regulation]. 323 95

A quantitative histochemical method (Trident) has been adapted to measure the activities of 4 enzymes, succinate dehydrogenase (SD), isocitrate dehydrogenase (ICD), glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6-PGD), within the liver acini of the rat during the postnatal developmental period. Quantitative changes of these enzymes in livers of rats of 25 g and 50 g body weight were studied, with particular emphasis on the activity-rest cycle. The results indicate a time-dependent heterogeneous distribution of enzymes along the acinar zones and the pattern of localization is age-dependent. When the mean enzyme activity from each group in relation to the time of the day are compared, a mirror image of each other could be seen. In general, a high enzyme activity has been observed during the resting phase in 25-g rats and low in 50-g rats. During the developmental period, the mean ICD activity is diminished, whereas G6PD and 6-PGD are augmented, and SD activity remains unchanged.
...
PMID:Quantitative topochemistry of rat liver enzymes during postnatal development in relation to activity-rest cycle. 382 86

The activities of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, isocitrate dehydrogenase, malic enzyme, lactate dehydrogenase and malate dehydrogenase have been determined in secreted milk from sows, rats and rabbits. Within each species, although there was considerable variation in the absolute activities of these enzymes, the relative activities were similar to those observed for, or previously published for mammary homogenates. The only exception was milk glucose 6-phosphate dehydrogenase which tended to lose activity upon prolonged storage in the mammary gland. These results suggest that the pattern of milk enzymes can be an accurate reflection of that occurring in the mammary gland.
...
PMID:NADP-linked dehydrogenases in secreted milk. 390 19

In porcine areolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an iron-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and iron transport.
...
PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---