July 1, 1984Journal of Experimental BiologyOpen Access

Differences in temperature dependence of muscle contractile properties and myofibrillar ATPase activity in a cold-temperature fish

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Population

Single muscle fibres isolated from the fast myotomal muscle of the teleost Myoxocephalus scorpius L. and…

Design

Preclinical

Authors

IJIA JohnstonUniversity of St Andrews BSBruce D. SidellIdaho State University

Discussion

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Implication

Temperature-dependent force rise in fish muscle extends ectotherm mechanics; leaves open translation to human cardiac contractility.

Structured PICO

Population

Single muscle fibres isolated from the fast myotomal muscle of the teleost Myoxocephalus scorpius L. and chemically skinned with 1% Brij, and Triton-X 100 extracted myofibrils

Intervention

Temperature variations (2 degrees C to 20 degrees C)

Outcome

Maximum Ca2+-activated force (P0), maximum contraction velocity (V0, Vmax), and Mg2+, Ca2+-ATPase activitysurrogate

The study demonstrates a lack of proportionality between unloaded contraction velocity and ATPase activity in fish muscle fibers across different temperatures, likely due to mechanical constraints.

Cite This Study

Johnston et al. (1984) studied this question.

synapsesocial.com/papers/6a7079a726a7f98052dcf9aa https://doi.org/10.1242/jeb.111.1.179

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Differences in temperature dependence of muscle contractile properties and myofibrillar ATPase activity in a cold-temperature fish

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Differences in temperature dependence of muscle contractile properties and myofibrillar ATPase activity in a cold-temperature fish

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider