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A protein that forms the microfilaments of the eukaryotic cytoskeleton and plays an important role in cell movement, shape, and internal organization. In muscle cells, it functions with myosin to produce contraction.

[Latin āctus, motion; see act + -in.]
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.


(Biochemistry) a protein that participates in many kinds of cell movement, including muscle contraction, during which it interacts with filaments of a second protein, myosin
[C20: from act + -in]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014


(ˈæk tən)

a protein that functions in muscular contraction by combining with myosin. Compare actomyosin.
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.actin - one of the proteins into which actomyosin can be split; can exist in either a globular or a fibrous form
actomyosin - a protein complex in muscle fibers; composed of myosin and actin; shortens when stimulated and causes muscle contractions
simple protein - a protein that yields only amino acids when hydrolyzed
Based on WordNet 3.0, Farlex clipart collection. © 2003-2012 Princeton University, Farlex Inc.
References in periodicals archive ?
This alteration in the physical structure is closely associated with the polymerization of globular or monomeric actin (G-actin) to filamentous actin (F-actin) that leads to secretion of substances into the surrounding medium [7].
Unreacted sea urchin sperm contain a membrane-bounded acrosomal vesicle at the apex, which sits atop a nuclear fossa (a depression in the nucleus--see below) containing a granular mass of unpolymerized globular actin (G-actin) surrounding the actomere.
Currently, it is not known in detail whether the binding capacity and/or affinity of Gc-globulin for G-actin is influenced by the loading with vitamin D and its metabolites.
Brownian dynamics (BD) simulations of the binding of the muscle form of fish fructose-l,6-bisphospahte aldolase (aldolase) to F-or G-actin confirm the strong interactions previously demonstrated in rabbit (3).
Cellular actin exists in two forms, filamentous polymerized actin (F-actin) and globular/monomer depolymerized actin (G-actin), and transitions between these forms during highly dynamic intracellular polymerization and depolymerization processes [8].
Previous studies demonstrated that actin polymerization, which is manifested by an increased ratio of F-actin to G-actin, and RhoA/ROCK activation were significantly increased in diabetic cardiomyocytes [22, 23].
To analyse the levels of F-actin and G-actin, liver samples were homogenized with PHEM buffer (60 mM Pipes, 20 mM HEPES, 10 mM EGTA, 2 mM Mg[Cl.sub.2],1% Triton X-100, and pH 7.0) and ultra-centrifuged (48.000 rcf) at 4[degrees]C for 5min to separate both fractions.
This probably depends on the use of F-actin and not G-actin as antigen in the ELISA: In vitro incubation of intestinal epithelial cells with gliadin caused intracellular actin polymerization with an increase in F-actin (2), which is the real neo-epitope recognized by AAAs.
Brownian dynamics (BD) simulations between LDH with previously built models of F-actin and G-actin (2) were performed.