Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis.

Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Research Abstract Details 

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Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Abstract Text:

K Oiwa,T Kawakami,H Sugi,

To obtain information about the mechanism of ATP-dependent actin-myosin sliding responsible for muscle contraction, we studied the "unitary" distance of sliding between a myosin-coated glass microneedle and actin filament arrays (actin cables) in a giant algal cell induced by iontophoretic application of ATP, attention being focused on the minimum distance of ATP-induced sliding when the amount of applied ATP was gradually decreased in the presence of hexokinase and D-glucose. The number of myosin heads interacting with actin cables was reduced to less than 100, as judged from the maximal force Po (approximately 100 pN) generated by myosin heads on the needle in the presence of 2 mM ATP. When the amount of iontophoretically applied ATP was decreased by reducing the amount of charge passed through the ATP electrode from 80 to 2 nC, the distance of ATP-induced actin-myosin sliding decreased almost linearly from approximately 100 to approximately 10 nm, no detectable actin-myosin sliding being observed with further reduction of the charge passed through the electrode. The amount of external load exerted by the bent microneedle was less than 1% of Po for the sliding distance < 50 nm. The actin-myosin sliding distances with a small amount of ATP slightly above the amount required to induce the minimum sliding distance were distributed around integral multiples of 10 nm, suggesting that the unitary distance of actin-myosin sliding coupled with ATP hydrolysis is of the order of 10 nm.

Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Publishing Authors By Initials

K Oiwa,T Kawakami,H Sugi,

For similar animals: chordata: vertebrates: mammals: lagomorpha: rabbits research abstracts see: animals: chordata: vertebrates: mammals: lagomorpha: rabbits research

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Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 114

Page Numbers: 28-32

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1993

Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Keywords Mesh Terms:

KEYWORDS: Rabbits

MESH TERMS: physiology

Chemical & Substance for Abstract: Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Unitary distance of actin-myosin sliding studied using an in vitro force-movement assay system combined with ATP iontophoresis.

AFFILIATION: Department of Physiology, School of Medicine, Teikyo University.

Country: JAPAN

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MEDLINETA: J Biochem

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