Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The response of rat gastrocnemius muscle fibers to chronic streptozotocindiabetes was studied. Transverse sections of this muscle from normal and diabetic rats were histochemically assayed for reduced diphosphopyridine nucleotide-diaphorase, myofibrillar adenosine triphosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, and alkaline phosphatase activities. Cross-sectional areas of the fiber types were measured, and fiber capillarization and populations estimated. Chemically-induced diabetes appeared to have little effect on the metabolic or morphological properties of slow-twitch fibers. However, a general dedifferentiation occurred in the 2 fast-twitch fiber populations. There was a loss of oxidative potential in the fast-twitch-oxidative-glycolytic fibers, and a significant decrease in size in the fast-twitch-glycolytic fibers. No change in the proportions of slow- and fast-twitch fibers in the muscles of diabetic rats occurred. It is concluded that hypoinsulinism has differential effects on the 3 fiber types in heterogeneous rat skeletal muscle, and that slow-twitch fibers are least affected by the diabetic condition.
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PMID:Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats. 12 6

The effects of vitamin E deficiency on membrane integrity were studied by examining the temperature dependence of membrane-bound enzyme activities in liver mitochondria and microsome and in muscle sarcoplasmic reticulum. In vitamin E-deficient rabbits, the specific activities at 37 degrees of mitochondrial oligomycin-sensitive ATPase (EC 3.6.1.3), beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30), and microsomal glucose-6-phosphatase (EC 3.1.3.9) were increased, whereas those of microsomal NADH cytochrome C reductase (EC 1.6.99.3) and sarcoplasmic reticulum Ca-ATPase were reduced in comparison to control rabbits. Arrhenius plots of activity against temperature yielded a linear plot over the range 10 to 40 degrees in the case of beta-hydroxybutyrate dehydrogenase, NADH cytochrome C reductase and Ca-ATPase, and multiple discontinuities for glucose-6-phosphatase and oligomycin-sensitive ATPase. In control rabbits, all five enzymes showed a single discontinuity in the Arrhenius plot over the range 16 to 19 degrees. These results reflect changes in the microenvironment of membrane-bound enzymes as a consequence of vitamin E depletion.
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PMID:Effects of vitamin E deficiency on the activities of lipid-requiring enzymes in rabbit liver and muscle. 22 Mar 97

A study of the ultrastructural localization of 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD), 11 beta-hydroxysteroid dehydrogenase (11 beta-HSD), glucose-6-phosphate dehydrogenase (G-6-PD), beta-hydroxybutyrate dehydrogenase (beta-HBD), NADH diaphorase (NADH-D) and NADPH diaphorase (NADPH-D) in the guinea-pig testis is reported. The procedures employed included short immersion or perfusion fixation with aldehydes followed by incubation of small blocks in a tetrazolium salt or a ferricyanide medium. The effects of incubation conditions were investigated, and a reaction medium for the ultracytochemical demonstration of 11 beta-HSD is described. Using suitable controls, evidence for the specificity of the cytochemical reactions is presented. It was found that all the enzymes studied were present in both the Leydig and Sertoli cells of the guinea-pig testis and that the intracellular distribution pattern for each enzyme was independent of the cell type. Using tetrazolium salt techniques, both 3 beta-HSD and 11 beta-HSD activities were localized on or in membranes of smooth endoplasmic reticulum and within the mitochondria. With the ferricyanide techniques, G-6-PD activity was found to be associated mainly with the smooth endoplasmic reticulum membranes, while beta-HBD activity was limited to mitochondria. With both the tetrazolium salt and ferricyanide techniques, the reaction products for NADH-D and NADPH-D activities showed localizations which were similar to those observed for the steroid dehydrogenases.
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PMID:The ultrastructural localization of the enzymes related to steroid hormone metabolism in the guinea-pig testis. 42 99

The effects of storage at low temperature on the transition in enzyme function, Tf*, and the Arrhenius activation energy, Ea, were determined for several enzymes associated with the inner membrane of rat liver mitochondria. The enzymes studied were succinate:cytochrome c reductase, cytochrome c oxidase, beta-hydroxybutyrate dehydrogenase, and oligomycin-sensitive, Mg2+-activated ATPase. For freshly isolated mitochondria the Tf*, for succinate:cytochrome c reductase and cytochrome c oxidase, occurred at approximately 23 degrees C and was coincident with a transition in structure, Ts*, determined as the change in temperature coefficient of motion for a spin label intercalated with the membrane lipids. This suggest that the change in thermal response of the membrane-associated enzymes is related to a change in molecular ordering of the membrane lipids. When mitochondria were stored at -12 degrees C, the specific activities of succinate:cytochrome c reductase and cytochrome c oxidase decreased. Concomitant with these changes the Ea, above Tf*, increased. After 100 days storage at -12 degrees C, Ea above Tf* approached the value for Ea below Tf* such that the transition in thermal response could no longer be detected. In contrast, for mitochondria stored at -196 degrees C, although the specific activity declined over the 100 days storage, no changes in either Ea or Tf* were evident. The results indicate a need for caution in evaluating comparative studies of Tf and Ea, for membrane-associated enzymes, using mitochondria which have been frozen and stored.
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PMID:The influence of storage temperature on the transition, activation enthalpy, and activity of enzymes associated with inner mitochondrial membranes. 282 42

Quantitative histochemical assays of several enzymes (succinic, lactic, beta-hydroxybutyrate, alpha-glycerophosphate, and glucose-6-phosphate dehydrogenases, NAD diaphorase, and phosphorylase) in the myocardium of persons who had died suddenly with postinfarctional cardiosclerosis have failed to reveal any changes specific for this patient group. Direct correlations were established between the enzyme activities assayed, on the one hand, and the extent of myocardial hypertrophy and the signs of chronic heart failure, on the other. The activities of beta-hydroxybutyrate dehydrogenase and glucose-6-phosphate dehydrogenase, which are involved in fatty acid utilization and in the pentose phosphate pathway, were elevated in cases of moderate hypertrophy, as were those of all redox enzymes in cases of strongly marked hypertrophy, although they were reduced in cases with signs of chronic cardiac failure despite the presence of considerable myocardial hypertrophy. Areas of acute myocardial ischemia were discovered in 45% of the cases.
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PMID:[Histochemical study of the enzyme activity of the myocardium of sudden death victims with postinfarct cardiosclerosis]. 296 Feb 98

NADH-diaphorase, succinate dehydrogenase (SDH), beta-hydroxybutyrate dehydrogenase (beta-HBDH), malate dehydrogenase (MDH) and cytochrome oxidase (CytO) were demonstrated histochemically in isolated perfused rat hearts during global ischaemia from 0 to 12 hours. The corresponding enzyme activities were measured when possible. The histochemically demonstrable activities of NADH-diaphorase and MDH decreased during the first hour of ischaemia. The time course of inactivation of biochemically detectable NADH-ferricyanide oxidoreductase was much the same as that of NADH-diaphorase. Both histochemically and biochemically detectable beta-HBDH gradually decreased by about 6 h of ischaemia. NADH-diaphorase but not MDH itself proved to be the rate-limiting factor when demonstrating MDH histochemically with nitroblue tetrazolium (NBT), whereas in the case of beta-HBDH the situation was probably the reverse. CytO and SDH activities did not change during the experimental period. Histochemistry clearly demonstrated ischaemic cellular injury, even though no significant diagnostic changes of ischaemia were visible by light microscopy. Even though this shows that enzyme-histochemical methods can be sensitive indicators of early ischaemic injury, in practice the time between the onset of injury and death as well as between death and autopsy must be taken into consideration when interpreting the results.
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PMID:Correlations between enzyme histochemical reactions and respective enzyme activities in global ischaemic rat hearts. 300 15

Growth of Mycobacterium phlei under low oxygen tension resulted in specific activities two to twenty times lower for formate dehydrogenase, malate dehydrogenase, beta-hydroxybutyrate dehydrogenase, lactate oxidase and NADH dehydrogenase than when cultures were grown under high aeration. An increase in fumarate reductase and succinate dehydrogenase occurred with M. phlei grown under low oxygen tension. Malate: vitamin K dehydrogenase and glucose-6-phosphate dehydrogenase activity were not significantly affected by the oxygen tension used to grow the bacteria, and neither culture contained a lactate dehydrogenase. With growth of M. phlei in conditions of low oxygen tension, cytochrome a was not detected, but cytochrome b was prominent in membranes and cytochrome c was present in the soluble fraction.
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PMID:Influence of oxygen tension on the respiratory activity of Mycobacterium phlei. 318 14

To evaluate the diagnostic role of histochemically demonstrated aerobic dehydrogenases in ischemic myocardial injury NADH-diaphorase, succinate dehydrogenase (SDH), beta-hydroxybutyrate dehydrogenase (HBDH) and malate dehydrogenase (MDH) were demonstrated histochemically and the corresponding enzyme activities were measured biochemically in isolated perfused rats hearts after global ischemia from 0 to 12 h. The present data show that the enzyme-histochemical methods when used properly are more sensitive indicators of early ischemic injury than classical histological staining procedures. From the enzymes tested here the histochemical demonstration of HBDH turned out to be best suited for use when suspecting ischemic myocardial injury at autopsy.
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PMID:Oxidative enzyme activities and respective histochemical reactions in ischemic rat myocardium. 342 4

To study changes in lipid-protein-interaction and fluidity in mitochondrial and microsomal membranes of brain during development and aging, the Arrhenius plots of marker enzymes for mitochondrial inner and outer membranes as well as those of microsomal membranes were compared at different ages. The enzymes were, beta-hydroxybutyrate dehydrogenase (BDH) for the inner mitochondrial membrane and rotenone-insensitive-NADH-cytochrome c reductase (Mit-NADH-CytR) for the outer membrane; also antimycin-insensitive-NADH-cytochrome c reductase (Micr-NADH-CytR) and NADPH-cytochrome c reductase for the microsomal membranes. The ages studied were, 1, 5, 30, 60 days postnatal and 2 years. In the microsomes, the plots of NADH-cytochrome c reductase were found to be biphasic at all ages except in the newborn where no break temperature was observed. The activation energy of this enzyme in the physiological range of temperature was found to be high in the newborn, declining with brain maturation. The plot of this enzyme in the old rat showed no difference when compared with the mature. The specific activity of the enzyme, however, was markedly reduced in the old brain microsomal fraction. In contrast, comparison of the plots of microsomal NADPH-cytochrome c reductase at the various ages revealed no break temperature and very similar energies of activation. For the inner mitochondrial membrane beta-hydroxybutyrate dehydrogenase, the Arrhenius plots were generally biphasic at all ages studied with a break temperature of about 20 degrees C. However, the newborn plot was only barely biphasic showing a high energy of activation in the physiological range of temperature. In contrast, for the outer membrane NADH-cytochrome c reductase, the newborn plots were definitely biphasic, exhibiting low activation energy above the breaks. There was also a significant decline in the break temperature with brain development. No significant differences in the plots of this enzyme were found between the old and mature brain cortex. It is concluded that the enzymes of inner and outer mitochondrial membranes as well as the oxidative enzymes of microsomal membranes may show differential patterns of change in lipid-protein-interaction during development and aging, the changes being more marked in development than in aging.
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PMID:Arrhenius plots of membrane-bound enzymes of mitochondria and microsomes in the brain cortex of developing and old rats. 373 27

Histochemical study of enzymatic activity in the myocardium was performed in sudden cardiac death. Human hearts in which there were no macroscopic and histological focal or diffuse changes served as material. The following enzymes were studied in the anterior or posterior walls of the left ventricle or in the interventricular septum: succinate dehydrogenase, lactate dehydrogenase (LDH), beta-hydroxybutyrate dehydrogenase (OHBDH), alpha-glycerophosphate- and glucose-6-phosphate dehydrogenase, NAD-diaphorase and phosphorylase. Increased activity of OHBDH and LDH was found: 36,0 and 22,6% higher than in trauma and brain hemorrhage that served as control. These alterations seem to be connected with the increase of blood content of fatty acids, and lactate as a response to the catecholamine excess. Foci of an acute ischemia were found in the interventricular septum in 80% of cases in which phosphorylase was revealed. The appearance of the ischemic foci was obviously due to the coronary arteries contraction.
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PMID:[Histoenzymological characteristics of the myocardium in sudden cardiac death]. 405 12


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