Rigor Tension Development in Excised "Rested", "Partially Exercised" and "Exhausted" Chinook Salmon White Muscle

1998 ◽  
Vol 63 (1) ◽  
pp. 48-52 ◽  
Author(s):  
A.R. JERRETT ◽  
A.J. HOLLAND
1963 ◽  
Vol 20 (1) ◽  
pp. 45-58 ◽  
Author(s):  
Hans Buttkus

The superficial red muscle of lingcod (Ophiodon elongatus) was shown to exhibit unique properties of post-mortem contraction and tension development. In comparison with white muscle, rigor contraction and isometric rigor tension in red muscle were about three times as great. The rate of contraction of the red muscle was dependent on temperature and also on the oxygen concentration in the surrounding atmosphere. The elastic modulus of the red muscle of trout and lingcod increased with increasing post-mortem time. Following the onset of rigor mortis a gradual increase in elasticity was observed. The maximum effects of contraction, tension and elasticity coincided with the onset of rigor mortis and each could therefore be used as a measure of this phenomenon. It was concluded from these experiments that stiffening of a fish with the onset of rigor mortis is not due to contraction or tension development of the muscles, but rather to their changing mechanical properties. A convenient measure of the changing mechanical properties in the muscle was the elastic modulus.Morphological differences between the very active, myoglobin rich, red muscle and the white muscle of lingcod were demonstrated by means of electron micrographs. The high glycogen content in the area of sarcoplasm of the red muscle, as indicated in electron micrographs, was confirmed by chemical analysis. Red muscle in rested fish was shown to contain from 1 to 3 times more glycogen than white muscle.


2010 ◽  
Vol 499 (1-2) ◽  
pp. 133-143 ◽  
Author(s):  
Leonard G. Forgan ◽  
Alistair R. Jerrett ◽  
Nicholas P.L. Tuckey ◽  
Malcolm E. Forster

1985 ◽  
Vol 63 (4) ◽  
pp. 811-816 ◽  
Author(s):  
Bruce D. Sidell ◽  
Ian A. Johnston

Maximum catalytic activity and thermal sensitivity of Mg2+–Ca2+ activated myofibrillar ATPase from either red or white muscle tissue of chain pickerel is unaffected by 4–6 weeks acclimation to temperatures of 5 or 25 °C. Arrhenius plots of myofibrillar ATPase activity from red muscle are linear over the entire range of assay temperatures (2–32 °C; Q10 = 3.3). Similar plots of white muscle ATPase activity show a pronounced discontinuity at approximately 10 °C and a much greater thermal sensitivity below this temperature (Q10 = 11.2) than above it (Q10 = 2.2). Thermal dependence of myofibrillar ATPase activity from white muscle does not accurately predict the effect of temperature upon contraction velocities of isolated white muscle fibers. Contraction velocity of single chemically skinned white muscle fibers was sevenfold less temperature sensitive than ATPase activity below the 10 °C transition and 1.6-fold less temperature sensitive above this temperature (Q10 (0–27 °C) = 1.6). Maximum Ca2+-activated tension development was particularly temperature independent (Q10 = 1.2), ranging from 14 ± 1.6 N/cm2 at 5 °C to 20.9 ± 2.1 N/cm2 at 25 °C. Power output chain pickerel muscle, a product of these two parameters (force × velocity), should therefore show a relatively low thermal dependence (Q10 < 2) over the normal range of habitat temperatures.


1987 ◽  
Vol 253 (3) ◽  
pp. C444-C455 ◽  
Author(s):  
R. Ventura-Clapier ◽  
V. A. Saks ◽  
G. Vassort ◽  
C. Lauer ◽  
G. V. Elizarova

Skinned rat papillary muscles and purified preparations of rat cardiac myofibrils were used to study the nature of the interaction of creatine kinase with cardiac myofibrils. High activity of creatine kinase (2 IU/mg protein in fibers and 0.9 IU/mg in purified myofibrils) was due mostly to reversibly bound enzyme. This activity could be removed and rebound. The process of creatine kinase rebinding was characterized by apparent Km value of 0.14 mg/ml (approximately equal to 2 X 10(6) M). Rebinding of creatine kinase to cardiac myofibrils restored the phenomenon of functional compartmentation of adenine nucleotides in myofibrillar space and restored the ability of phosphocreatine to decrease the rigor tension in the presence of MgADP. The physiological experiments with quick length changes showed that rebinding of creatine kinase to skinned papillary muscle also restored Ca sensitivity, increased maximal tension development, decreased stiffness, and restored the tension recovery after quick length changes in muscle under condition of inhibition of endogenous creatine kinase by 1-fluoro-2,4-dinitrobenzene. It is concluded that creatine kinase reversibly bound to cardiac myofibrils is involved in the energy supply for cardiac contraction.


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