Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have shown that dietary provision of carbohydrate can alter cardiac isomyosin distribution in hormonally deficient rats. The main objective of this study was to determine if varying the heart's potential to utilize carbohydrate for energy provision can influence the cardiac isomyosin expression in normal weanling rats. Animals were assigned to one of five groups according to dietary and/or metabolic treatment: (1) mixed-control--(M); (2) high carbohydrate--(H); (3) low carbohydrate--(L); (4) mixed-diet supplemented with oxfenicine, a cardiospecific fatty acid oxidation inhibitor--(MO); and (5) high carbohydrate diet supplemented with oxfenicine--(HO). The results show that 4 weeks of dietary manipulations aimed to either increase or decrease carbohydrate supply to the heart, failed to induce any alterations in either cardiac myosin ATPase activity or isoenzyme pattern. However, extremes in carbohydrate provision altered the metabolic properties of both heart and skeletal muscle. A low carbohydrate diet increased 3-hydroxyacyl CoA dehydrogenase (P less than 0.05) and citrate synthase activities (P less than 0.05) and decreased glycogen content in both heart and soleus muscle; whereas, a high carbohydrate diet, in conjunction with oxfenicine, tended to increase hexokinase activity in these same tissues. These alterations provide indirect evidence that the contributions of both fat and carbohydrate to the energy balance of the heart and skeletal muscle were altered by the imposed dietary interventions. Collectively, these results suggest that although the substrate utilization patterns of the normal weanling heart can be modified via dietary manipulation, such shifts do not exert any regulatory influence on cardiac isomyosin expression.
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PMID:Dietary effects on cardiac metabolic properties in rodents. 214 63

Skeletal limb muscles of the dog could generally be differentiated into three fibre types according to myosin adenosine triphosphatase (ATPase) (pH 9.4) and succinic dehydrogenase activities. However, because this was not always possible, for comparative purposes only, division into low myosin ATPase (slow twitch) type I and high myosin ATPase (fast twitch) type II fibres was used. The percentage of these fibre types in m deltoideus, m triceps brachii caput longum, m vastus lateralis, m gluteus medius, m biceps femoris and m semitendinosus was examined in the greyhound, crossbred and foxhound. In all muscles the greyhound had a significantly higher percentage of fibres with high myosin ATPase activity at pH 9.4 than the other breeds, with almost 100 per cent in most muscles examined. The activities of nine enzymes and glycogen concentration were determined in m gluteus medius and m semitendinosus of the greyhound and crossbred. Significantly higher levels of creatine kinase, aldolase, alanine aminotransferase and citrate synthase and significantly lower activities of 3-hydroxyacyl coenzyme A dehydrogenase and hexokinase were found in both muscles of the greyhound. The implications of these findings are discussed.
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PMID:Skeletal muscle fibre composition in the dog and its relationship to athletic ability. 645 29

Muscle biopsies of the vastus lateralis muscle taken before and after 18 weeks of resistance training were compared by preparing frozen cross sections for electron microscopy and using adjacent sections for fiber typing by myosin ATPase activity. Quantitative ultrastructural changes were observed in histochemically-identified muscle fiber types of twelve young women who underwent the training. The percentage of type IIB fibers decreased and IIA fibers increased. The cross-sectional area of all major fiber types increased with training. The absolute volume of myofibrils, intermyofibrillar space, and mitochondria increased with training for most major fiber types (type I, IIA and IIAB), but the relative volume percentages were not significantly changed because of corresponding fiber hypertrophy. Mean mitochondrial size for types I and IIA and myofibril size for types IIC and IIB increased significantly with training. The capillary number per fiber and density did not change with training. Activity levels were measured for selected glycolytic and oxidative enzymes. Cytochrome oxidase and hexokinase increased significantly with training, while creatine kinase, citrate synthase, phosphofructokinase, glyceraldehyde phosphate dehydrogenase and hydroxyacyl CoA dehydrogenase enzymes were not significantly altered. The results suggest that this type of high-repetition resistance training causes the intracellular components of all fiber types to increase proportionally with an increase in fiber size. In addition, the enzyme analysis indicates the muscle as a whole may increase its oxidative phosphorylation capacity in conjunction with the decreased percentage of type IIB fibers.
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PMID:Muscle fiber types of women after resistance training--quantitative ultrastructure and enzyme activity. 825 33

The aim of this study was to evaluate myofibrillar creatine kinase (EC 2.7.3.2) activity on the background of the effect of substrate channeling by myosin ATPase and to compare it with creatine kinase (CK) activity of whole skinned fibers. In order to assess CK activity, skinned fibers were prepared from the rat psoas major muscles defined by light microscopy. The activity in permeabilized fibers after treatment with saponin, Triton X-100 and Ca(2+)-free medium reached 2.80, 6.97 and 3.32 micromol ATP min(-1) mg(-1) protein, respectively, when a coupled enzyme assay system with external hexokinase and glucose-6-phosphate dehydrogenase was used. Transmission electron microscopy (TEM) revealed a possible interference among activities of sarcolemmal, sarcoplasmic, myofibrillar and mitochondrial CK from persisting structures. For evaluation of the myofibrillar CK itself, a pure myofibrillar fraction was prepared. Fraction purity was confirmed by TEM and by enzymatic assays for marker enzymes. Two procedures, i.e. the coupled enzyme assay and the evaluation of phosphocreatine (PCr) concentration before and after the CK reaction, were used for measurement of CK activity in this fraction. The procedures resulted in 3.2 nmol ATP min(-1) mg(-1) protein and 7.6 nmol PCr min(-1) mg(-1) protein, respectively. These alternative approaches revealed a discrepancy between the reacting portions of PCr by more than 50 %, which provides information about the size of the effect, generally described as substrate channeling.
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PMID:Creatine kinase reaction in skinned rat psoas muscle fibers and their myofibrils. 1047 Aug 63

Kinases and ATPases produce adenosine diphosphate (ADP) as a common product, so an assay that detects ADP would provide a universal means for activity-based screening of enzymes in these families. Because it is known that most kinases accept ATPbetaS (sulfur on the beta-phosphorous) as a substrate in place of adenosine triphosphate (ATP), the authors have developed a continuous assay using this substrate, with detection of the ADPbetaS product using dithio reagents. Such an assay is possible because dithio groups react selectively with ADPbetaS and not with ATPbetaS. Thiol detection was done using both Ellman's reagent (DTNB) and a recently developed fluorescent dithio reagent, DSSA. Therefore, the assay can be run in both absorbance and fluorescence detection modes. The assay was used to perform steady-state kinetic analyses of both hexokinase and myosin ATPase. It was also used to demonstrate the diastereoselectivity of hexokinase (R) and myosin ATPase (S) for the isomers of ATPbetaS, consistent with previous results. When run in fluorescence mode using a plate reader, an average Z' value of 0.54 was obtained, suggesting the assay is appropriate for high-throughput screening.
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PMID:A dithio-coupled kinase and ATPase assay. 1694 91