The in vitro motility assay parameters of actin filaments from Mytilus edulis exposed in vivo to copper ions

2009 ◽  
Vol 491 (1-2) ◽  
pp. 32-38 ◽  
Author(s):  
Natalia N. Vikhoreva ◽  
Petr G. Vikhorev ◽  
Maria A. Fedorova ◽  
Ralf Hoffmann ◽  
Alf Månsson ◽  
...  
Keyword(s):  
Mytilus Edulis ◽  
Actin Filaments ◽  
Copper Ions ◽  
Motility Assay ◽  
In Vitro Motility Assay ◽  
In Vitro Motility

scholarly journals A simple method for measuring the relative force exerted by myosin on actin filaments in the in vitro motility assay: evidence that tropomyosin and troponin increase force in single thin filaments

2000 ◽  
Vol 350 (3) ◽  
pp. 693-699 ◽  
Author(s):  
Wu BING ◽  
Adam KNOTT ◽  
Steven B. MARSTON
Keyword(s):  
Actin Filaments ◽  
Isometric Force ◽  
Critical Concentration ◽  
Isometric Tension ◽  
Motility Assay ◽  
In Vitro Motility Assay ◽  
Simple Method ◽  
In Vitro Motility ◽  
Muscle Tropomyosin

We have studied the effect of an internal load on the movement of actin filaments over a bed of heavy meromyosin (HMM) in the invitro motility assay. Immobilized α-actinin can bind to actin filaments reversibly and ultimately stop the filaments from moving. Above a critical concentration of α-actinin, thin filament velocity rapidly diminished to zero. The fraction of thin motile filaments decreased linearly to zero with increasing α-actinin concentration. The concentration of α-actinin needed to stop all filaments from moving (0.8µg/ml with actin) was very consistent both within and between experiments. In the present study we have defined the ‘index of retardation’ as the concentration of α-actinin needed to stop all filament movement, and we propose that this index is a measure of the isometric force exerted by HMM on actin filaments. When we measured the effect of immobilized α-actinin on motility in the presence of 10mM Pi we found that the index of retardation was 0.62±0.07 (n = 3) times that in the absence of Pi. This observation is in agreement with the reduction of isometric tension in chemically-skinned muscle due to Pi. In a series of comparative experiments we observed that tropomyosin and troponin increase the index of retardation and that the degree of increase depends upon the tropomyosin isoform studied. The index of retardation of actin is increased 1.8-fold by skeletal-muscle tropomyosin, and 3-fold by both cardiac-muscle and smooth-muscle tropomyosin. In the presence of troponin the index of retardation is 2.9–3.4-fold greater than that of actin with all tropomyosin isoforms.

scholarly journals Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca 2+-sensitivity of Actin-Myosin Interaction

Acta Naturae ◽  
2013 ◽  
Vol 5 (3) ◽  
pp. 126-129 ◽  
Author(s):  
D. V. Shchepkin ◽  
A. M. Matyushenko ◽  
G. V. Kopylova ◽  
N. V. Artemova ◽  
S. Y. Bershitsky ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Myosin Head ◽  
Motility Assay ◽  
Published Data ◽  
Physiological Effects ◽  
Sliding Velocity ◽  
In Vitro Motility Assay ◽  
In Vitro Motility ◽  
Myosin Interaction

We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са 2+ concentrations and the Са 2+-sensitivity of the actin-myosin interaction underlying this sliding. Based on an analysis of the recently published data on the structure of the actin-Tmmyosin complex, we suppose that the physiological effects of these mutations in Tm can be accounted for by their influence on the interactions between the central part of Tm and certain sites of the myosin head.

Caged FEDA-ATP: a new tool in the measurement of ATP turnover during the in vitro motility assay

1995 ◽  
Vol 23 (3) ◽  
pp. 401S-401S ◽  
Author(s):  
Daren S. Jeffreys ◽  
Robert J. Eaton ◽  
Clive R. Bagshaw
Keyword(s):  
Motility Assay ◽  
In Vitro Motility Assay ◽  
In Vitro Motility ◽  
Atp Turnover

scholarly journals An automated in vitro motility assay for high-throughput studies of molecular motors

Lab on a Chip ◽  
2018 ◽  
Vol 18 (20) ◽  
pp. 3196-3206 ◽  
Author(s):  
Till Korten ◽  
Elena Tavkin ◽  
Lara Scharrel ◽  
Vandana Singh Kushwaha ◽  
Stefan Diez
Keyword(s):  
High Throughput ◽  
Molecular Motors ◽  
Lab On A Chip ◽  
Force Generation ◽  
Motility Assay ◽  
In Vitro Motility Assay ◽  
In Vitro Motility ◽  
Cargo Transport

Molecular motors, essential to force-generation and cargo transport within cells, are invaluable tools for powering nanobiotechnological lab-on-a-chip devices.

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