scholarly journals Mechanical properties of skinned rabbit psoas and soleus muscle fibres during lengthening: effects of phosphate and Ca2+.

1992 ◽  
Vol 451 (1) ◽  
pp. 503-523 ◽  
Author(s):  
G J Stienen ◽  
P G Versteeg ◽  
Z Papp ◽  
G Elzinga
Keyword(s):  
Mechanical Properties ◽  
Soleus Muscle ◽  
Muscle Fibres ◽  
Rabbit Psoas

scholarly journals Mechanical Properties of Demembranated Flight Muscle Fibres from a Dragonfly

1991 ◽  
Vol 159 (1) ◽  
pp. 135-147
Author(s):  
M. PECKHAM ◽  
D.C. S. WHITE
Keyword(s):  
Mechanical Properties ◽  
Flight Muscle ◽  
Muscle Length ◽  
Psoas Muscle ◽  
Muscle Fibres ◽  
Active Tension ◽  
Rabbit Psoas ◽  
King's College ◽  
Flight Muscles ◽  
Drury Lane

The mechanical properties of demembranated muscle fibres of synchronous flight muscle from a dragonfly Libellula quadrimaculata, asynchronous flight muscle from the giant waterbug Lethocerus indicus and synchronous psoas muscle from rabbit were compared in relaxed, active and rigor conditions. The properties were compared to the known structure and protein compositions of these muscles. We found that active tension of L. indicus flight muscles was stretch-activated (tension was low and was significantly increased following a rapid stretch of 1 % of muscle length), whereas both dragonfly flight muscle and rabbit psoas muscle were not (active tension was high and did not significantly increase following a rapid stretch of 1%). Three different properties have been suggested to give rise to stretch activation in asynchronous muscles: (1) a matching of the helix periodicities of actin target sites to myosin crossbridge heads, (2) a special form of troponin subunit called troponin-H, and (3) the high resting stiffness of these muscles inducing strain in the thick filaments. Rabbit psoas muscle has none of these properties. Dragonfly flight muscles do not have the helix matching, but they do have a form of troponin-H and a high resting stiffness. It seems most likely that dragonfly flight muscles are not stretch-activated because they do not have the helix matching. Note: Present address: Department of Biophysics, King's College London, 26–29 Drury Lane, London, WC2B 5RL, UK.

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