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:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Frozen sections of the pectoral, gastrocnemius and cardiac muscles from seven different species of birds were stained for myofibrillar ATPase and for succinic dehydrogenase. Several methods of myofibrillar ATPase were used including different pre-incubation treatments. Myofibrillar ATPases were also measured biochemically and the pH profile of the activity was compared with the histochemical staining following pre-incubation at different pH. Myofibrils from the different muscles were also subjected to sodium dodecyl sulphate acrylamide gel electrophoresis in order to separate the low molecular weight components of myosin. The results demonstrated that histochemical methods can be applied, with a reasonable degree of confidence, to classifying fibres in avian muscles although the classification used for mammalian muscles needs to be modified. They also showed that avian muscles, particularly the pectoralis, varies considerably between species and their mode of locomotion.
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PMID:A combined histochemical and biochemical study of myofibrillar ATPase in pectoral, leg and cardiac muscle of several species of bird. 3 55

Histochemical techniques have been employed to characterize enzymatic activity in the mesocoxal muscles of the cockroach, Periplaneta americana. Through our studies of the enzymes myosin-ATPase, NADH reductase, succinic dehydrogenase (SDH), and lactic dehydrogenase (LDH), we were able to classify fibers within these muscles according to criteria established for muscle fibers of vertebrates. Many of the mesocoxal muscles possess two different and distinct populations of fibers, whereas the remaining muscles are homogeneous with respect to their constituent fibers. The data presented here indicate biochemical heterogeneity for muscles of differing structural and functional features and possible neurotrophic influences upon oxidative enzymes and myosin-ATPase isozymes.
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PMID:Enzyme histochemistry of the mesocoxal muscles of Periplaneta americana. 3 9

Muscle samples were obtained from the gastrocnemius of 17 female and 23 male track athletes, 10 untrained women, and 11 untrained men. Portions of the specimen were analyzed for total phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) activities. Sections of the muscle were stained for myosin adenosine triphosphatase, NADH2 tetrazolium reductase, and alpha-glycerophosphate dehydrogenase. Maximal oxygen uptake (VO2max) was measured on a treadmill for 23 of the volunteers (6 female athletes, 11 male athletes, 10 untrained women, and 6 untrained men). These measurements confirm earlier reports which suggest that the athlete's preference for strength, speed, and/or endurance events is in part a matter of genetic endowment. Aside from differences in fiber composition and enzymes among middle-distance runners, the only distinction between the sexes was the larger fiber areas of the male athletes. SDH activity was found to correlate 0.79 with VO2max, while muscle LDH appeared to be a function of muscle fiber composition. While sprint- and endurance-trained athletes are characterized by distinct fiber compositions and enzyme activities, participants in strength events (e.g., shot-put) have relatively low muscle enzyme activities and a variety of fiber compositions.
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PMID:Skeletal muscle enzymes and fiber composition in male and female track athletes. 12 49

Sera raised against actin and myosin, extracted from white muscle of fish, were used for the immune-histochemical characterization of muscle fibers. It appeared that both, the actin- and the myosin serum are specific for white muscle fibres in fish. Further it was found that in both, the A- and the I-band of the sacromeres, fibre type specific proteins are present. The classification of muscle fibre types obtained with the antisera was compared with the classification obtained with some enzyme histochemical reactions. Muscle fibres that reacted positively with the two sera, also showed a high histochemical myofibrillar ATP-ase activity. The correlation with a low succinate dehydrogenase- and a high lactate dehydrogenase activity was not always found.
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PMID:Muscle fibre typing with sera against myosin and actin. A comparison between enzyme- and immunohistochemical classification. 13 46

1. The development of the characteristic histochemical appearance of the slow anterior latissimus dorsi (ALD) and fast posterior latissimus dorsi (PLD) was studied in chickens during embryonic development as well as during regeneration of minced muscle. 2. During embryonic development the activity of the oxidative enzyme succinic dehydrogenase (SDH) is higher in the slow ALD muscle already at 16 days of incubation. At this time the fast PLD has a higher activity of the glycolytic enzyme, phosphorylase. Although the histochemical appearance of the two types of muscle is already different at 16 days, their contractile speeds are still similar. No difference in myosin ATP-ase was found in the two muscles in young embryos but in 20-day old embryos the two muscles became distinctly different when stained for this enzyme. 3. When PLD muscles in hatched chickens redeveloped during regeneration in place of ALD the histochemical characteristics of the regenerated muscle resembled ALD, and when ALD regenerated in place of PLD it resembled PLD. 4. It is concluded that the histochemical characteristics of slow and fast muscles become determined during early development, even before any difference in contractile properties can be detected and that they are determined by the nerve.
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PMID:Differentiation of slow and fast muscles in chickens. 14 31

Single muscle fibres were isolated by microdissection from freeze-dried samples of rabbit psoas and soleus muscles. The individual fibres were typed according to qualitative histochemical reactions for succinate dehydrogenase or NADH-tetrazolium reductase and for alkaline Ca2+-activated myofibrilla myosin ATPase after acid or alkaline preincubation. Methods are described for electrophoretic analysis by means of polyacrylamide disc electrophoresis in the presence of SDS of total myofibrilla proteins in single fibres after pre-extraction of soluble proteins. Fast-twitch white fibres revealed a myosin light chain pattern characteristic of "fast- type" myosin with three light chains of apparent molecular weights of 22,300 (LC1) 18,400 (LC2) and 16,000 (LC3). Fast-twitch red fibres were indistinguishable in this respect from fast-twist white fibres and showed an identical pattern of myosin light chains. Slow-twitch fibres could be characterized by a myosin light chain pattern typical of myosin of slow-twitch muscles with peptides of the apparent molecular weights of 23,500 (LC1Sa), 23,000 (LC1Sb) and 18,500 (LS2S). Slow-twitch fibres isolated from soleus as well as from psoas muscle were indistinguishable with regard to their myosin light chain patterns, thus suggesting that fibres of the same histochemical type correspond in their myosin light chain patterns irrespective of their origin from different muscles.
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PMID:Myosin light chain patterns of individual fast and slow-twitch fibres of rabbit muscles. 14 18

Histochemical profiles of individual muscle fibres were established using myosin adenosine triphosphatase (myosin ATPase), succinate dehydrogenase (SDHase), and glycogen phosphorylase (GPase) reactions in three muscles (semitendinosus, diaphragm, and pectoralis transversus) of the horse and dog. The major histochemical difference between fibres lies in their myosin ATPase activity; fibres can be subdivided into those with a high and those with a low activity. In horse muscle, all fibres have a high activity of GPase. In the diaphragm and pectoralis transversus, all fibres have a high SDHase activity, but fibres with a low activity of SDHase are also present in samples of the semitendinosus. In dog muscle, all fibres have a high SDHase activity; myosin ATPase low-reacting fibres also have a low activity of GPase. There is a greater fractional area of myosin ATPase high-reacting fibres in the pectoralis transversus and semitendinosus of thoroughbred horses and greyhounds (breeds selected for high speed running) and in the diaphragm of greyhounds. In adults this feature does not appear to be due to training, as are the differences in aerobic and anaerobic capacity (shown in other studies). The preponderance of myosin Atpase high-reacting fibres suggests that there may be differences in the nervous systems of athletes and non-athletes. It is concluded that the proportions of fibre types in muscles are related to the functions of muscles and of their parts. No sex differences or detraining effects were apparent, although the value for the proportion of fibre types (as differentiated by the myosin ATPase reaction) in the limb muscles of thoroughbred crosses lies between those of thoroughbreds and non-thoroughbreds.
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PMID:Differences in the histochemical properties of skeletal muscles of different breeds of horses and dogs. 15 95

The plasmalemma and hyaline ectoplasm together constitute the sensory and motor organ of macrophages. The purpose of this study was to isolate this cell fraction in order to analyze it biochemically and functionally. Brief sonification of warmed rabbit lung macrophages caused release of heterodisperse hyaline blebs and filopodia, which were easily collected by differential centrifugation. Viewed in the electron microscope, these structures consisted of membrane-bounded sacs principally containing actin filaments. Some contained secondary lysosomes. They were enriched threefold over whole cell homogenates in specific adenylate cyclase activity and in trichloroacetic-acid-precipitable (125)I when derived from cells labeled with 125(I) by means of a lactoperoxidase-catalyzed reaction. These markers were found to have identical isopycnic densitites when macrophage homogenates were subjected to sedimentation in a focusing sucrose density gradient system, and these markers had densities distinct from those of other cytoplasmic organelles. These markers were therefore assumed to be associated with macrophage plasma membranes. The specific beta- glucuronidase activity of the bleb fraction was similar to that of homogenates, but the blebs had considerably lower specific succinic dehydrogenase activity and RNA content, and DNA was undetectable. Electrophoresis of blebs solubilized in sodium dodecyl sulfate on polyacrylamide gels revealed polypeptides co-migrating with macrophage actin-binding protein, myosin, and actin; blebs also had EDTA-activated adenosine triphosphatase activity characteristic of myosin. The concentrations of actin-binding protein and myosin were higher in blebs than in cells or cytoplasmic extracts, whereas actin concentrations were similar (relative to extracts) or only slightly greater (than in cells). Blebs and intact cells had high lactate dehydrogenase activities in the presence but not the absence of Triton X-100. Blebs and cells oxidased 1-[(14)C]glucose, and the rate of glucose oxidation was increased substantially in the presence of latex beads. We conclude that intact sacs of plasmalemma encasing contractile proteins and cytoplasmic enzymes can be isolated from macrophages. They are enriched in myosin and actin-binding protein, indicating that the contractile apparatus is regulated in the cell periphery. These structures have the capacity to respond to environmental signals. We suggest the name "podosomes" for them because of their resemblance to macrophage pseudopodia. We propose that podosome formation results from rapid dissolution of the cortical gel when the membrane is in an actively extended configuration.
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PMID:Peripheral hyaline blebs (podosomes) of macrophages. 92 88

Mitochondrial respiration, succinate dehydrogenase coenzyme Q reductase, and myosin B were investigated in ischemic myocardium from experimental myocardial infarction in dogs. Respiratory control ratio of mitochondria was impaired by ischemia at 60 min after coronary ligation, and oxygen consumption was inhibited 120 min later. Enzyme activity of succinate dehydrogenase coenzyme Q reductase was decreased at 6 hr after coronary ligation. Calcium ion sensitivity of myosin B declined 12 hr after coronary ligation. However, adenosine triphosphatase activity of myosin A from infarcted myocardium was not different from that of the intact one. These results suggest that interaction in the sequence of enzyme complexes was first impaired in ischemic myocardium and that deterioration of enzyme activity was then manifested.
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PMID:Relationship between energy liberation and utilization in ischemic cardiac muscle. 103 51

Morphological and enzymatic responses in fibers expressing fast, slow, or both types of myosin heavy chain (MHC) were studied in rats after 14 days of spaceflight (COSMOS 2044) or hindlimb suspension. Although the percentage of slow-twitch fibers was unchanged, a higher percentage of fibers that expressed both slow and fast MHC was observed in flight and suspended rats than in synchronous ground-based controls. The soleus was 25 and 34% smaller than control after 14 days of flight and suspension, with the reduction in fiber cross-sectional area (CSA) being greater in slow- than in fast-twitch fibers in both experimental groups. The activities of succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) were not significantly affected by flight or suspension. The total SDH activity (i.e., SDH activity x CSA) decreased significantly in the slow-twitch fibers of the flight and the fast-twitch fibers of the suspended rats, in large part due to fiber atrophy. A shift in MHC expression in 14 and 9% of the fibers in flight and suspended rats occurred without a change in myosin adenosinetriphosphatase activity. The SDH and GPD activities of the fibers that expressed both slow and fast MHC were slightly higher than the slow-twitch fibers and slightly lower than the fast-twitch fibers. These data indicate that events were initiated within 14 days of spaceflight or suspension that began to reconfigure the protein profiles of 9-14% of the slow-twitch fibers from typical slow-twitch toward those of fast-twitch fibers, while all fibers were dramatically losing total protein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Rat soleus muscle fiber responses to 14 days of spaceflight and hindlimb suspension. 138 48


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