scholarly journals Energy metabolism in single human muscle fibres during intermittent contraction with occluded circulation.

1993 ◽  
Vol 460 (1) ◽  
pp. 443-453 ◽  
Author(s):  
P L Greenhaff ◽  
K Söderlund ◽  
J M Ren ◽  
E Hultman
1982 ◽  
Vol 333 (1) ◽  
pp. 227-249 ◽  
Author(s):  
S. G. Cull-Candy ◽  
R. Miledi ◽  
O. D. Uchitel

1973 ◽  
Vol 44 (4) ◽  
pp. 12P-13P
Author(s):  
Eric Hultman

1992 ◽  
Vol 49 (1) ◽  
pp. 110-115 ◽  
Author(s):  
S. Hinterleitner ◽  
M. Huber ◽  
R. Lackner ◽  
W. Wieser

Juveniles of the zooplanktivorous Danube bleak (Chalcalburnus chalcoides mento) and of the benthivorous nase (Chondrostoma nasus) were subjected to an endurance training regime for 81–90 d. Growth performance was better in trained than in untrained Danube bleak but not in nase. Mass specific heart size was significantly greater in trained than in untrained C. nasus, but no difference was found in C. chalcoides. The size of muscle fibres increased with training in both species; in nase the red and pink fibres and in Danube bleak the red and white fibres exhibited the most conspicuous response. Mass specific activities of the enzymes of energy metabolism were generally not affected by training, but in the white fibres of C. chalcoides, three glycolytic enzymes displayed a parallel trend indicating an increase of the glycolytic potential with training of about 25%. Since the Danube bleak maintains an irregular, burst-like mode of swimming even under the endurance training regime, we assume the lactate produced intermittently in the white muscles to be oxidized in the heart and the red muscles. The activities of three glycolytic heart enzymes were up to 25-fold higher in C. chalcoides than in C. nasus.


2001 ◽  
Vol 86 (3) ◽  
pp. 411-415 ◽  
Author(s):  
C. Karatzaferi ◽  
A. de Haan ◽  
W. van Mechelen ◽  
A. J. Sargeant

1990 ◽  
Vol 240 (1297) ◽  
pp. 197-210 ◽  

Immunolabelling with a 5 nm gold probe was used to localize dystrophin at the ultrastructural level in human muscle. The primary antibody was monoclonal, raised against a segment (amino acids 1181-1388) from the rod domain of dystrophin. The antibody (Dy4/6D3) is specific for dystrophin and shows no immunoreactivity with any protein from mdx mouse muscle or from patients with a gene deletion spanning part of the molecule recognized by the antibody (Nicholson et al . 1989 a ; England et al . 1990). Using this antibody, labelling was almost entirely confined to a narrow 75 nm rim at the periphery of the muscle fibres. Histograms of the distance from the gold probe to the cytoplasmic face of the plasma membrane and of the distance between gold probes (nearest neighbour in a plane parallel with the plasma membrane) displayed modes at approximately 15 nm and 120 nm, respectively. The distribution of the probe was the same in longitudinal and transverse sections of the muscle. These observations suggest that the rod portion of the dystrophin mole­cule is normally arranged close to the cytoplasmic face of the plasma membrane and that the molecules form an interconnecting network. Labelling was not associated with the transverse tubular system.


2012 ◽  
Vol 22 ◽  
pp. S15
Author(s):  
L. Boldrin ◽  
J.E. Morgan

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