Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Skeletal muscle samples were obtained by needle biopsy from two depths of the m. gluteus medius of 50, young race-trained thoroughbred racehorses. Histochemical and biochemical characteristics of the muscle samples were analysed. Fibres were classified as type I, type IIa or type IIb on the basis of the pH dependent lability of the myosin ATPase reaction. The activities of citrate synthase (CS) and glycogen phosphorylase (Phos) were determined. Muscle fibre composition varied markedly between deep and superficial muscle samples and this was reflected in differences in the activities of citrate synthase (CS) and phosphorylase (Phos). CS activity was greater in samples taken from a depth of 90 mm (deep) than those taken from a depth of 40 mm (superficial: 122 +/- 19 compared with 88 +/- 16 mumol/g dry muscle/min at 25 degrees C). Phos activity was greater in superficial samples (137 +/- 20) compared with deep samples (117 +/- 21). Regression analysis was used to estimate the enzyme activities in the different fibre types. No significant correlations were observed between histochemical and biochemical measures and subsequent racing performance.
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PMID:Skeletal muscle characteristics in 2 year-old race-trained thoroughbred horses. 791 52

Muscle fibre type composition and distribution in the biceps brachii (long head) and triceps brachii (long head) of the rat and rabbit were investigated using the following histochemical techniques: myosin ATPase, with preincubation at pH 10.4 and 4.35; succinate dehydrogenase (SDH) and glycogen phosphorylase. The muscle fibres were classified into slow-twitch (SO), fast-twitch glycolytic (FG), fast-twitch oxidative glycolytic (FOG and FOg) and fast-twitch oxidative fibres (FO). Significant differences in the regional distribution of muscle fibre types have been observed between the rat and the rabbit. In the rat, SO fibres were restricted to the deep regions of both biceps and triceps brachii, whereas FG fibres were located in the intermediate and superficial regions (the superficial regions contained the highest percentages of FG fibres). In the rabbit, SO and FG fibres were spread over the entire muscle, although SO and FG fibres were most abundant in the deep and superficial regions respectively. These findings indicate that the biceps and triceps brachii are more regionalised in the rat than in the rabbit.
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PMID:Muscle fibre types and their distribution in the biceps and triceps brachii of the rat and rabbit. 964 21

Ageing is associated with a reduction in muscle carnosine (beta-alanyl-L-histidine), but there are no data on the changes specifically in type I and type II muscle fibres. Given the higher carnosine content of type II fibers, changes observed in whole muscle may be secondary to a shift in fibre composition. Carnosine, beta-alanine, histidine, taurine, and citrate synthase (CS) and glycogen phosphorylase (Phos), were measured in pools of single muscle fibres from freeze-dried muscle biopsies of vastus lateralis of nine elderly sedentary subjects (65-80 years) with osteoarthritis of the knee and undergoing total knee replacement, and nine young moderately active healthy subjects (20-35 years). Fibres were characterised as type I or II by myosin ATPase activity. Carnosine was 53.2% lower in type II fibres of older subjects resulting in an estimated 7% (and most probably still higher) decline in intracellular physico-chemical buffering capacity. Younger subjects showed higher CS activities in type I and higher Phos activities in type II fibres. These differences were less apparent in elderly subjects. Possible causes for the change in the carnosine content are reduced physical activity, reduced meat intake, or the result of progressive denervation.
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PMID:Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects. 1696 7