RetroSearch Browse

Home - News ( United States | United Kingdom | Italy | Germany ) - Football scores

Showing content from https://pubmed.ncbi.nlm.nih.gov/3386748/ below:

Force measurements by micromanipulation of a single actin filament by glass needles

. 1988 Jul 7;334(6177):74-6. doi: 10.1038/334074a0. Force measurements by micromanipulation of a single actin filament by glass needles

Affiliations

Affiliation

¹ Department of Biophysical Engineering, Osaka University, Japan.

PMID: 3386748
DOI: 10.1038/334074a0

Item in Clipboard

Force measurements by micromanipulation of a single actin filament by glass needles

A Kishino et al. Nature. 1988.

. 1988 Jul 7;334(6177):74-6. doi: 10.1038/334074a0. Affiliation

¹ Department of Biophysical Engineering, Osaka University, Japan.

PMID: 3386748
DOI: 10.1038/334074a0

Item in Clipboard

Abstract

Single actin filaments (approximately 7 nm in diameter) labelled with fluorescent phalloidin can be clearly seen by video-fluorescence microscopy. This technique has been used to observe motions of single filaments in solution and in several in vitro movement assays. In a further development of the technique, we report here a method to catch and manipulate a single actin filament (F-actin) by glass microneedles under conditions in which external force on the filament can be applied and measured. Using this method, we directly measured the tensile strength of a filament (the force necessary to break the bond between two actin monomers) and the force required for a filament to be moved by myosin or its proteolytic fragment bound to a glass surface in the presence of ATP. The first result shows that the tensile strength of the F-actin-phalloidin complex is comparable with the average force exerted on a single thin filament in muscle fibres during isometric contraction. This force is increased only slightly by tropomyosin. The second measurement shows that the myosin head (subfragment-1) can produce the same ATP-dependent force as intact myosin. The magnitude of this force is comparable with that produced by each head of myosin in muscle during isometric contraction.

PubMed Disclaimer

Cited by

Mechanotransduction in the renal tubule.
Weinbaum S, Duan Y, Satlin LM, Wang T, Weinstein AM. Weinbaum S, et al. Am J Physiol Renal Physiol. 2010 Dec;299(6):F1220-36. doi: 10.1152/ajprenal.00453.2010. Epub 2010 Sep 1. Am J Physiol Renal Physiol. 2010. PMID: 20810611 Free PMC article. Review.

RetroSearch is an open source project built by @garambo | Open a GitHub Issue

Search and Browse the WWW like it's 1997 | Search results from DuckDuckGo

HTML: 3.2 | Encoding: UTF-8 | Version: 0.7.3