meromyosin


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Related to meromyosin: light meromyosin

meromyosin

 [mer″o-mi´o-sin]
a fragment of the myosin molecule isolated by treatment with proteolytic enzyme; there are two types, heavy (H-meromyosin) and light (L-meromyosin).

mer·o·my·o·sin

(mer'ō-mī'ō-sin),
A subunit of the tryptic digestion of myosin; two types are produced, H-meromyosin and L-meromyosin.

meromyosin

(mĕr′ə-mī′ə-sĭn)
n.
Either of two subunits (designated heavy and light) of a myosin molecule, as obtained through the action of a proteolytic enzyme such as trypsin.

mer·o·my·o·sin

(mer'ō-mī'ō-sin)
A subunit of the tryptic digestion of myosin; two types are produced, H-meromyosin and L-meromyosin.
References in periodicals archive ?
(2007) Calcium inhibition of Physarum myosin as examined by the recombinant heavy meromyosin. In Regulatory Mechanisms of Striated Muscle Contraction (eds.
N-Ethylmaleimide modified heavy meromyosin: a probe for actomyosin interactions.
The authors reported that the actomyosin complex is pulled in the direction of meromyosin fraction of the main myosin helix.
(29) In addition, a useful motility assay was introduced by observing the sliding of microtubules on dynein molecules absorbed on a glass surface, as in the case of kinesin or heavy meromyosin. (30)
Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay.
In the Characean cell, cortical fibrils were confirmed to be composed of actin filament bundles by observation of the arrowhead structure formed by binding with skeletal muscle heavy meromyosin. (3,4) Myosin was thought to be contained in the streaming endoplasm, and putative Chara myosin was verified by observation under a dark field microscope that cortical fibrils moved actively on the glass surface when the cytoplasm was squeezed in an artificial medium.
Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J.
Myosin molecules are built from light and heavy (H) meromyosins, and H-meromyosin contains the ATPase and myosin actin-combining property (Lawrie, 1979).