Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intrafusal fibres from the rat soleus were investigated for representative histochemical profiles in sedentary animals and animals chronically exercised for 17 weeks on a treadmill. The pattern of myosin adenosine triphosphatase (ATPase) activity in the polar region revealed three intrafusal fibre types: (1) myosin ATPase-dark (MD) fibres, alkali- and acid-stabile; (2) myosin ATPase-light (ML) fibres, alkali- and acid-labile; and (3) myosin ATPase-reversible (MR) fibres, alkali-stabile and acid-labile. The three fibre types were correlated with the level of reduced NADH diaphorase activity, with MR, ML and MD fibres staining dark, moderate and light, respectively. In the equatorial region the morphological features of representative ML and MD fibres revealed that they were nuclear bag fibres, while representative MR fibres were identified as nuclear chain fibres. The MR fibres in the exercised animals had higher levels of myosin ATPase alkaline stability and acid lability than MR fibres in the sedentary animals, suggesting the MR fibre profiles are selectively influenced by chronic exercise. The mean cross-sectional area of MR fibres from the exercised animals was significantly less than the MR fibres from the sedentary animals. In contrast to the effect of endurance training on NADH diaphorase activity in extrafusal muscle fibres, there was evidence of less activity in the MD fibres of the exercised animals.
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PMID:Histochemical profiles of rat soleus intrafusal fibres after chronic exercise. 12 93

The muscle fiber types and sizes in the M. stapedius (middle ear muscle) of the domestic chicken, Gallus gallus were determined histochemically on the basis of their reactions to myofibrillar adenosine triphosphatase (mATPase), succinic dehydrogenase and NADH diaphorase. Only type II fibers were identified at pH 9.4 and 4.2. At pH 4.6 three levels of activity were seen: high, intermediate and low. With the staining techniques three subtypes of fibers for oxidative enzymes, Types II1 (highly glycolytic), II12 (intermediately glycolytic and lipolytic) and II123 (highly lipolytic) were identified. Fiber diameter was also measured for the different fiber types. The average fiber diameter was around 20 micron for each fiber type. Although similar in size, the fiber types were markedly different in their histochemical properties. These findings plus those of earlier physiological studies suggest that the M. stapedius of G. gallus is a fast twitch, muscle with fibers of similar diameter showing mainly fatigue resistance characteristics.
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PMID:A histochemical characterization of muscle fiber types in the avian M. stapedius. 288 51

Endogenous enzyme activity can be readily and routinely demonstrated in ultrathin, frozen sections for electron microscopy. The procedure employed to obtain the best structural preservation as well as enzyme activity in thin sections involved fixation in glutaraldehyde, embedding in thiolated gelatin or pure gelatin, partial dehydration in glycerol, and sectioning in a cryostat at -35 degrees C with a slightly modified Porter-Blum microtome on which the tissue is maintained at -70 degrees C and the knife at -23 degrees C. Kidney cortex was used as test tissue, but a few other organs were occasionally used. Thin sections were floated on the surface of several incubation media routinely employed for enzyme cytochemistry. Positive, specific reactions were obtained for alkaline phosphatase in kidney brush border, for adenosine triphosphatase in brush border and in basal membranes of distal tubules, for acid phosphatase and esterase in lysosomes, and for NADH diaphorase in mitochondria. Mitochondrial ATPase was sporadically evident only in the distal tubule of the kidney. Localizations of enzyme activity reported by other technical approaches were confirmed and in some cases somewhat improved.
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PMID:Ultrathin frozen sections. II. Demonstration of enzymic activity. 429 6

The morphology of the tongue muscles was studied by in situ dissection as well as by histological and histochemical methods. By means of the latter an anatomical reassessment of attachments and fiber courses was made. The histochemistry was studied in sections stained for myofibrillar adenosine triphosphatase (mATPase), succinic dehydrogenase, NADH diaphorase, phosphorylase, esterase, glycogen and lipids. Fibers of type I and type II were identified, and the latter were subdivided into II1 (highly glycolytic), II12 (intermediately glycolytic and lipolytic) and II123 (highly lipolytic). In the extrinsic muscles, the fibers were 19-25% type I (mean diameter 27 micrometers) and 75-81% type II (37 micrometers); the three type II subgroups appeared in equal proportions, each accounting for 22-30% of the total fiber amount. Pars longitudinalis superior m. hyoglossi and pars longitudinalis inferior m. styloglossi contained only type II fibers, mainly type II12 (67% and 46%, respectively), of diameters like those in m. hyoglossus and m. styloglossus. The intrinsic muscles also consisted entirely of type II fibers (23 micrometers). II123 fibers predominated in m. verticalis (83%), which has only 10% H12 and 6% II1, whereas the fiber composition of m. transversus was more balanced: 37% type II1, 32% II12 and 31% II123.
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PMID:Morphological and histochemical properties of tongue muscles in cat. 645 24