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)

Capillary supply, the proportion of oxidative fibres and blood flow were studied in fast rat muscles (tibialis anterior, TA, and extensor digitorum, EDL) made ischaemic by ligation of the common iliac artery, in chronically stimulated muscles and in ischaemic chronically stimulated muscles. Stimulation was carried out for 6 h/day at 10 Hz (three periods of 2 h with 90-120-min intervals between stimulations) for 10-12 days using electrodes implanted in the vicinity of the lateral popliteal nerve. Blood flow (measured by radioactive microspheres) was 3.62 +/- 0.52 ml.100 g-1.min-1 at rest and 78.4 +/- 14.6 ml.100 g-1.min-1 (mean +/- SEM) during isometric contractions at 4 Hz. Ischaemic muscles had significantly lower blood flow at rest as well as during contractions (72 +/- 14% and 25 +/- 4% of the values in contralateral muscles respectively). Stimulated muscles had significantly higher flow than contralateral control muscles during contractions; stimulated ischaemic muscles had normal blood flow at rest, but the increase in flow during contractions was limited to a similar extent to that in ischaemic muscles alone. Of all anatomically present capillaries (staining for alkaline phosphatase in frozen sections) the capillary/fibre ratio increased by 36% in stimulated tibialis anterior, but was not significantly different from control muscles in stimulated ischaemic TA and was even lower than in control muscles in stimulated ischaemic EDL. The proportion of fast oxidative fibres (estimated on the basis of histochemical staining for myosin ATPase and succinate dehydrogenase) increased from 53.2 +/- 3.2% in normal EDL to 82.0 +/- 2.3% in chronically stimulated EDL and to 100% in chronically stimulated ischaemic muscles.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The role of blood flow and/or muscle hypoxia in capillary growth in chronically stimulated fast muscles. 170

Biopsies of the human masseter muscle were made using an intraoral approach. Sections were cut in a cryostat and freeze-dried. Using the myosin ATPase method at pH 9.3 the recognized heterogeneity of the muscle with respect to type I and type II fibers was confirmed. Sections were examined in an SEM by the method of energy dispersive X-ray analysis using a computer assisted semi-quantitative method (bulk analysis-thick sections) to determine the distribution of Na, P, S, Cl and K and their relative masses. Element concentrations in descending order were K, S, P, Na and Cl. Some element ratios were compared with results in the literature for other muscle (biochemical and microprobe analysis) and found to be generally in reasonable agreement. The results form a basis for the study of a prominent and accessible masticatory muscle in altered states.
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PMID:Microprobe analysis of human masseter muscle biopsies. 661 11

The size and quality of muscle specimens obtained by use of a percutaneous biopsy technique were studied. All biopsies were performed under local anesthesia, using an 11-gauge biopsy needle. The mean +/- SEM size of specimens obtained from 128 biopsies of the semitendinosus muscles of 16 Alaskan Huskies was 23.8 +/- 4.4 mg. All biopsy specimens were of sufficient quality to permit histochemical differentiation of the fiber types by use of myosin ATPase staining. An additional 8 biopsy specimens were obtained from 1 dog and analyzed for muscle glycogen content. These specimens contained 50.6 +/- 7.2 mmol of glucose/kg of muscle wet weight. This modified biopsy procedure was free of notable complications, and repeatable use produced specimens of adequate size and quality for histologic and biochemical analysis. It is concluded that this procedure is a safe and reliable alternative to open biopsy for diagnosis and management of neuromuscular, metabolic, and nutritional myopathies.
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PMID:New approach to percutaneous muscle biopsy in dogs. 853 88