myofibril


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Related to myofibril: myofilament, sarcoplasmic reticulum

myofibril

[¦mī·ō′fī·brəl]
(cell and molecular biology)
A contractile fibril in a muscle cell.
(invertebrate zoology)
References in periodicals archive ?
It is well known that, salt not only aids the solubility of meat proteins but also promotes the swelling of myofibrils.
2]--involved in muscle energy metabolism, glycolytic pathway in ATP generation, and organization of myofibril, respectively, that were downregulated differentially with the increase in storage time and were related particularly to K value, texture, color, and sensory characteristics.
Many of these sarcomeres are connected in a well-ordered series to form myofibrils that span from one muscle end to the other.
We previously established that, using skinned muscle fibers placed in a Ca buffer, each sarcomere exhibited stable auto-oscillation of contraction and elongation under the fixed Ca concentration of approximately 1 uM, through careful measurements of muscle fiber tension (especially using thin bundles of myofibrils ~1 um in diameter); we termed this phenomenon as spontaneous oscillatory contraction (SPOC) (see recent review by S.
Myofibrils bear most of the resting tension in frog skeletal muscle.
Histology of heart of DXR-treated animals showed loss of myofibrils and focal cytoplasmic vacuolization.
Hearts from SHS-treated rats stained with Masson trichrome showed extensive fibrosis and myofibril disarray at the 200X magnification (Figure 1C).
The effect of projectin's absence or reduction on IFM myofibril assembly is also investigated by immunofluorescence microscopy on pupal and adult samples.
While a number of viruses are capable of causing rhabdomyolysis in humans, the significance of myofibril damage associated with viral infections of the lung has not been well described.
The thin protein filaments located with the myofibril of the muscle.
Objective: A diverse variety of medical or lifestyle conditions lead to a progressive loss of muscle force by functionally impairing myofibril contractility and causing ultimately myofibril loss.
2002) found that during cooking, denaturation and melting of the endomysium as well as denaturation of the myofibril led to the loss of water holding capacity in BR meat protein, and thus, moisture in BR meat was easily released after cooking.