Resistance to fatigue of single muscle fibres from Xenopus related to succinate dehydrogenase and myofibrillar ATPase activities

1991 ◽  
Vol 76 (4) ◽  
pp. 589-596 ◽  
Author(s):  
WJ van der Laarse ◽  
J Lannergren ◽  
PC Diegenbach
Keyword(s):  
Succinate Dehydrogenase ◽  
Muscle Fibres ◽  
Single Muscle ◽  
Myofibrillar Atpase

scholarly journals Twitch and Tetanic Tension during Culture of Mature Xenopus laevis Single Muscle Fibres

2001 ◽  
Vol 109 (5) ◽  
pp. 410-417 ◽  
Author(s):  
R.T. Jaspers ◽  
H.M. Feenstra ◽  
M.B.E. Lee-de Groot ◽  
P.A. Huijing ◽  
W.J. van der Laarse
Keyword(s):  
Xenopus Laevis ◽  
Muscle Fibres ◽  
Single Muscle ◽  
Tetanic Tension

Absolute values of myothermic measurements on single muscle fibres from frog

1986 ◽  
Vol 7 (4) ◽  
pp. 327-332 ◽  
Author(s):  
N. A. Curtin ◽  
J. V. Howarth ◽  
J. A. Rall ◽  
M. G. A. Wilson ◽  
R. C. Woledge
Keyword(s):  
Muscle Fibres ◽  
Single Muscle

scholarly journals Caffeine and the contractility of single muscle fibres from the barnacleBalanus nubilus

1977 ◽  
Vol 269 (2) ◽  
pp. 421-439 ◽  
Author(s):  
C. C. Ashley ◽  
J. C. Ellory ◽  
P. J. Griffiths
Keyword(s):  
Muscle Fibres ◽  
Single Muscle

scholarly journals The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle

2001 ◽  
Vol 204 (15) ◽  
pp. 2627-2635 ◽  
Author(s):  
Berit Brüstle ◽  
Sabine Kreissl ◽  
Donald L. Mykles ◽  
Werner Rathmayer
Keyword(s):  
Molecular Mass ◽  
Thin Filament ◽  
Troponin I ◽  
Extensor Muscle ◽  
Apparent Molecular Mass ◽  
Muscle Fibres ◽  
Single Pair ◽  
Myofibrillar Proteins ◽  
Single Muscle ◽  
Western Blots

SUMMARYIn the isopod Idotea emarginata, the neuropeptide proctolin is contained in a single pair of motoneurones located in pereion ganglion 4. The two neurones supply dorsal extensor muscle fibres of all segments. Proctolin (1μmoll−1) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10mmoll−1 caffeine. In western blots of myofibrillar proteins isolated from single muscle fibres and treated with an anti-phosphoserine antibody, a protein with an apparent molecular mass of 30kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin I.

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