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:1.9.3.1 (cytochrome oxidase)
8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antisera were raised to acetyl-CoA carboxylase and 6-phosphogluconate dehydrogenase from mammary glands of lactating rabbits, and cytochrome oxidase from rat liver. The enzymes were all highly purified but gave rise to multispecific antisera when tested against tissue extracts. Absorption procedures were devised to free the antisera of contaminating antibodies. Antisera to acetyl-CoA carboxylase and cytochrome oxidase were absorbed with fractions discarded during enzyme purification. The antiserum to 6-phospho-gluconate dehydrogenase was absorbed with a tissue extract from an early stage in mammary-gland differentiation. Monospecific antisera are essential for enzyme turnover studies and therefore antisera should be extensively tested and absorbed before use. A general procedure for the absorption of antisera to purified enzymes has been devised on the basis of accepted principles of antisera absorption.
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PMID:Absorption of antisera for studies on specific enzyme turnover. 1 81

At present soluble NADP-dependent dehydrogenases are histochemically demonstrated in three different ways: according to the standard method incubation in aqueous media leads to the precipitation of formazan, the formation of which depends entirely on the presence of endogeneous NADPH2-tetrazolium reductases. With the two more recently established methods these reductases are by-passed with the use of intermediate electron acceptors incorporated in the medium. In addition, enzyme diffusion is inhibited either by an increased viscosity of the medium (PVA) or by a semipermeable membrane separating the medium from the section. Depending on the technique applied different distribution patterns have been described. By altering the concentrations of substrates, coenzyme, tetrazolium salt and cytochrome oxidase inhibitor, it was possible to improve both the PVA and membrane methods. Although similar results were obtained, because of its advantages the PVA method is recommended in this report and a detailed description is given. Using the latter for the demonstration of glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), malic enzyme (ME) and isocitrate dehydrogenase (ICDH), characteristic distribution patterns were obtained in the liver parenchyma of male and female rats. For the first time a high G6PDH activity could be demonstrated in nonparenchymal cells which are mainly found in zone 1 of the liver acinus.
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PMID:NADP-dependent dehydrogenases in rat liver parenchyma. I. Methodological studies on the qualitative histochemistry of G6PDH, 6PGDH, malic enzyme and ICDH. 2 20

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49

Hepatocytes were prepared from 15 degrees C acclimated catfish (Ictalurus punctatus) and maintained in primary culture for 20 days on biomatrix at 7, 15, and 25 degrees C without hormones or serum to determine if cells can directly adapt to temperature. Specific activities of cytochrome-c oxidase, NADH-cytochrome c reductase, citrate synthase, and glucose-6-phosphate dehydrogenase showed acclimatory rate compensation (7 greater than 15 greater than 25 degrees C cultured); 6-phosphogluconate dehydrogenase had activity changes of 15 greater than 7 greater than 25 degrees C cultured; activity of lactate dehydrogenase occurred in the series 7 greater than 15 = 25 degrees C. Protein synthesis of freshly isolated hepatocytes from catfish acclimated to the three temperatures exhibited acclimatory rate compensation. In contrast, protein synthesis of cultured hepatocytes occurred in the series 15 greater than 25 greater than 7 degrees C cultured. Protein degradation was highest at 25 degrees C followed by cells at 15 and 7 degrees C. Cultured hepatocytes showed incomplete temperature acclimation in vitro by way of enzyme activity changes and of protein synthesis. This suggests that some factor(s), such as hormones, is probably necessary to mediate the full temperature-acclimation process.
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PMID:Can cultured teleost hepatocytes show temperature acclimation? 300 35

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.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

1. Following acclimation of channel catfish to a reduction in temperature from 25 degrees to 15 degrees C, there were approximately two-fold increases in liver mass, cell size, total protein, and total enzyme activity, relative to activity per milligram of protein and per gram wet weight of tissue, indicating tissue hypertrophy. There was no change in either total liver DNA content or protein concentration per gram weight. 2. Green sunfish, unlike catfish, showed virtually no change in liver mass following cold acclimation. However, sunfish showed a net increase in total liver protein content and an increase in protein concentration. The increase in protein content was balanced by a reciprocal and equivalent decrease in glycogen content. Consequently, liver mass was maintained. 3. During cold acclimation both catfish and sunfish showed an increase in ventricular heart mass and protein content, but no change in protein concentration. 4. The activities of several enzymes were measured in liver from 15 degrees C and 25 degrees C steady-state-acclimated catfish and at intervals following transfer from 15 degrees to 25 degrees C and from 25 degrees to 15 degrees C. Total tissue enzyme activity showed positive compensation which correlated with the change in liver mass and protein content. Specific activities based on protein and on wet weight showed dissimilar acclimatory patterns. Two enzymes - cytochrome oxidase and lactate dehydrogenase - showed inverse compensation in specific activity but positive compensation in total activity. Citrate synthase, glucose-6-phosphate-dehydrogenase and 6-phosphogluconate dehydrogenase showed positive compensation in both specific and total activities. 5. The increase in tissue protein content or 'protein hypertrophy' occurred with cell hypertrophy in cold-acclimated catfish, while protein hypertrophy occurred as an increased protein concentration without cell hypertrophy in sunfish. This phenomenon is considered adaptive in that it permits a compensatory increase in the total enzymatic capacity of a tissue. The two-fold increases in total enzyme activities, superimposed on either an increase or decrease in specific activity, suggest that two biochemical mechanisms may be operative during cold-induced liver hypertrophy, one effecting a specific step in protein translation at a point common to the synthesis of all proteins and a second targetted pretranslationally, i.e., transcriptional regulation.
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PMID:Cold-acclimation-induced protein hypertrophy in channel catfish and green sunfish. 317 Aug 25

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.
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PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41

Enzyme histochemical methods were performed on sporozoite infected liver tissue of rats in order to gain insight into the nutrition and metabolism of exoerythrocytic forms of Plasmodium berghei. The following enzymes were demonstrated in the hepatocytic stages of the parasites, obtained 41 and 48 h after inoculation of sporozoites: acid phosphatase, cytochrome oxidase, NADH-tetrazolium reductase, succinate dehydrogenase, NAD+ and NADP+ dependent isocitrate dehydrogenase, NADP+-dependent malate dehydrogenase, lactate dehydrogenases, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenases and alpha-glycerol-phosphate dehydrogenase. The results suggest that a conventional Embden-Meyerhoff pathway, pentose phosphate pathway and Krebs' citric acid cycle may in part be present in these exoerythrocytic parasites. Alkaline phosphatase, nucleoside polyphosphatase, 5' nucleotidase, glucose-6-phosphatase, alpha-glucan phosphorylase, NAD+ dependent malate dehydrogenase, amino-peptidase M and non-specific esterases were not detected by our techniques in the parasite. The enzyme distribution of this intrahepatocytic malaria parasite revealed by histochemistry is compared with the enzyme distribution in the other phases of the parasite's life cycle.
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PMID:Histochemical observations on the exoerythrocytic malaria parasite Plasmodium berghei in rat liver. 608 94

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, 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 most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35

Channel catfish were collected on 11 different dates from October 1991 to July 1993 and acclimated in the laboratory to 7 degrees C, 15 degrees C, or 25 degrees C for 6 wk. Hepatosomatic index, mg protein mg-1 DNA, total liver DNA and protein, and the activities of liver glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase, and malate dehydrogenase were measured to examine seasonal variation in the acclimation response. Liver and muscle cytochrome oxidase and lactate dehydrogenase activities were measured to compare tissue-specific responses. Hepatosomatic indexes of fall and winter channel catfish were highest at 7 degrees C, with values at 15 degrees C higher than at 25 degrees C, while spring and summer fish had the highest values at 15 degrees C, with values at 7 degrees C higher than those at 25 degrees C. Acclimation patterns for total liver protein and DNA, mg protein mg-1 DNA, and glycogen were generally higher in cold temperatures but varied seasonally in an unpredictable manner. Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and malate dehydrogenase demonstrated positive acclimation in the fall and winter; fish collected in the spring and summer showed little or inverse acclimation. Liver lactate dehydrogenase activity showed little or no positive compensation at any time of the year. Cytochrome oxidase activity showed positive acclimation in muscle but not liver. All liver enzymes, even those that showed marginal acclimation on a protein basis, showed positive acclimation when activity was expressed on a whole-liver basis.
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PMID:Seasonal variations in the temperature acclimation response of the channel catfish, Ictalurus punctatus. 923 74


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